Byssal proteins of the freshwater zebra mussel,Dreissena polymorpha

The freshwater zebra mussel (Dreissena polymorpha) is a notorious biofouling organism. It adheres to a variety of substrata underwater by means of a proteinaceous structure called the byssus, which consists of a number of threads with adhesive plaques at the tips. The byssal proteins are difficult to characterize due to extensive cross-linking of 3,4-dihydroxyphenylalanine (DOPA), which renders the mature structure largely resistant to protein extraction and immunolocalization. By inducing secretion of fresh threads and plaques in which cross-linking is minimized, three novel zebra mussel byssal proteins were identified following extraction and separation by gel electrophoresis. Peptide fragment fingerprinting was used to match tryptic digests of several gel bands against a cDNA library of genes expressed uniquely in the mussel foot, the organ which secretes the byssus. This allowed identification of a more complete sequence of Dpfp2 (D. polymorpha foot protein 2), a known DOPA-containing byssal protein, and a partial sequence of Dpfp5, a novel protein with several typical characteristics of mussel adhesive proteins.     

Fluorescence methods for the histochemical demonstration of monoamines

Summary The histochemical fluorescence method of Falck and Hillarp for the demonstration of catecholamines and certain tryptamines, e.g. 5-hydroxytryptamine is based on the principle that these amines can be condensed with formaldehyde to yield strongly fluorescent 6,7-dihydroxy-3,4-dihydroisoquinolines and 6-hydroxy-3,4-dihydro--carbolines respectively. The investigation here reported presents the fluorescence characteristics and relative fluorescence yields for formaldehyde treated biogenic monoamines and certain related compounds enclosed in a dried protein layer. The fluorescence properties of some synthetic 6,7-substituted-3,4-dihydroisoquinolines and 3,4-dihydro--carbolines are given, and the fluorescence characteristics in relation to the molecular structure are discussed.Abbreviations used A adrenaline - DA dopamine - DOPA 3,4-dihydroxyphenylalanine - DOPS 3,4-dihydroxyphenyl-serine - 5-HT 5-hydroxytryptamine - 5-HTP 5-hydroxytryptophan - 5-MT 5-methoxytryptamine - -m-DA -methyl-dopamine - -m-DOPA -methyl-3,4-dihydroxyphenylalanine - -m-NA -methyl-noradrenahne - MTA 3-methoxy-tyramine - NA noradrenaline - NM normetanephrine - T Tryptamine - Try Tryptophan     

Catecholamines and related o-diphenols in cockroach hemolymph and cuticle during sclerotization and melanization: comparative studies on the order Dictyoptera

Summary Catecholamines and related o-diphenols extracted from the cuticle and hemolymph of adult cockroaches during sclerotization and pigmentation of the cuticle were analyzed by reverse phase HPLC with electrochemical detection. At ecdysis, dopamine (DA) oconjugates predominated in the hemolymph of Periplaneta americana, P. australasiae, P. fuliginosa, P. brunnea, and Blatta orientalis (Blattidae); Blattella germanica (Blattellidae); and Gromphadorhina portentosa and Blaberus craniifer (Blaberidae). n-Acetyldopamine (NADA) conjugates were second in abundance in these species, but were major in the hemolymph of the other blaberoid species, Leucophaea maderae and Nauphoeta cinerea. After ecdysis NADA became the major hemolymph catecholamine in all species as DA decreased rapidly. n--Alanyldopamine (NBAD) concentrations in the hemolymph remained low in all species, although NBAD and its metabolite, n--alanylnorepinephrine (NBANE), were generally the major catecholamines in tanning cuticle. Catechol (1,2-dihydroxybenzene) occurred mainly as a conjugate(s) at high levels in the hemolymph of nymphs and adults of all blattid species. Only trace amounts were detected in B. germanica and Cryptocercus punctulatus (Cryptocercidae), and none was found in any of the blaberoid species. High concentrations of NBANE and NBAD accumulated in tanning cuticle of B. germanica, G. portentosa, and all blattid species, whereas NADA and DA predominated in cuticle from the other blaberoid species, particularly L. maderae and N. cinerea. However, cockroaches as a group appear to utilize both the n-acetyl and n--alanyl catecholamines for stabilization of the exoskeleton. The Blattidae differed most from the other families in having considerably higher concentrations of catecholamines in hemolymph and cuticle, as well as the large amounts of catechol conjugates in the hemolymph.Abbreviations AMD -methlydopa - DA dopamine - DOBA 3,4-dihydroxybenzoic acid - DOPA 3,4-dihydroxyphenylalanine - DOPAC 3,4-dihydroxyphenylacetic acid - DOPET 3,4-dibydroxyphenylethanol - DOPKET 3,4-dihydroxyphenylketoethanol - HPLC high performance liquid chromatography - NADA n-acetyldopamine - NANE n-acetylnorepinephrine - NBAD n--alanyldopamine - NBANE n--alanylnorepinephrine - NE notepinephrine Contribution No. 90-88-J from the Kansas Agricultural Experiment Station, Kansas State University, Manhattan, KS. Cooperative investigation between the KAES and the ARS, USDA. K.J. Kramer is a research chemist and Adjunct Professor at the U.S. Grain Marketing Research Laboratory and Kansas State University, respectively. Address reprint requests to T.L. Hopkins     

Glycosylated Hydroxytryptophan in a Mussel Adhesive Protein from Perna viridis

The 3,4-dihydroxyphenyl-l-alanine (Dopa)-containing proteins of mussel byssus play a critical role in wet adhesion and have inspired versatile new synthetic strategies for adhesives and coatings. Apparently, however, not all mussel adhesive proteins are beholden to Dopa chemistry. The cDNA-deduced sequence of Pvfp-1, a highly aromatic and redox active byssal coating protein in the green mussel Perna viridis, suggests that Dopa may be replaced by a post-translational modification of tryptophan. The N-terminal tryptophan-rich domain of Pvfp-1 contains 42 decapeptide repeats with the consensus sequences ATPKPW₁TAW₂K and APPPAW₁TAW₂K. A small collagen domain (18 Gly-X-Y repeats) is also present. Tandem mass spectrometry of isolated tryptic decapeptides has detected both C²-hexosylated tryptophan (W₁) and C²-hexosylated hydroxytryptophan (W₂), the latter of which is redox active. The UV absorbance spectrum of W₂ is consistent with 7-hydroxytryptophan, which represents an intriguing new theme for bioinspired opportunistic wet adhesion.The amino acid 3,4-dihydroxyphenyl-l-alanine (Dopa)³ occurs in many proteins of the mussel holdfast or byssus (1, 2) and has recently been incorporated into mussel-inspired synthetic polymers with versatile adhesive consequences (3–7). One byssal protein in particular, mussel foot protein-1 (Mfp-1), has been investigated from over 15 mussel byssi, where it protectively coats compliant collagen-like proteins in the thread core (8–11). Mfp-1s typically contain 10–15 mol % Dopa in a highly conserved repeating peptide structure (8). In the blue mussel Mytilus edulis fp-1 (Mefp-1), for example, the consensus decapeptide AKPSYPPTYK is repeated over 70 times in tandem, and much of the tyrosine (Y) is converted to Dopa (Y*) (Fig. 1). In stark contrast to this, only trace levels of Dopa were detected in Pvfp-1 from the green mussel Perna viridis (Linnaeus 1758) (12), a notoriously invasive fouling species originally from the Indo-Pacific region (13). Because P. viridis fp-1 (Pvfp-1) and its homologue, Mefp-1, are both strongly aromatic, quinogenic, and composed of highly polar decapeptide repeats (12), identifying the Dopa-mimetic substitutes in Pvfp-1 has been a matter of considerable interest.Open in a separate windowFIGURE 1.The common blue mussel M. edulis and green mussel P. viridis are shown with attached byssal threads. Distinct consensus decapeptide repeat sequences are associated with the repeat domains in fp-1 foot proteins of the two species. The amino acid Dopa (Y*, right panel) is prominent in mefp-1 repeats but absent from Pvfp-1. O denotes trans-4-hydroxyprolines. Residues denoted as X₁ and X₂ are shown by this study to be derived from tryptophan.     

Novel Proteins Identified in the Insoluble Byssal Matrix of the Freshwater Zebra Mussel

The freshwater zebra mussel, Dreissena polymorpha, is an invasive, biofouling species that adheres to a variety of substrates underwater, using a proteinaceous anchor called the byssus. The byssus consists of a number of threads with adhesive plaques at the tips. It contains the unusual amino acid 3, 4-dihydroxyphenylalanine (DOPA), which is believed to play an important role in adhesion, in addition to providing structural integrity to the byssus through cross-linking. Extensive DOPA cross-linking, however, renders the zebra mussel byssus highly resistant to protein extraction, and therefore limits byssal protein identification. We report here on the identification of seven novel byssal proteins in the insoluble byssal matrix following protein extraction from induced, freshly secreted byssal threads with minimal cross-linking. These proteins were identified by LC-MS/MS analysis of tryptic digests of the matrix proteins by spectrum matching against a zebra mussel cDNA library of genes unique to the mussel foot, the organ that secretes the byssus. All seven proteins were present in both the plaque and thread. Comparisons of the protein sequences revealed common features of zebra mussel byssal proteins, and several recurring sequence motifs. Although their sequences are unique, many of the proteins display similarities to marine mussel byssal proteins, as well as to adhesive and structural proteins from other species. The large expansion of the byssal proteome reported here represents an important step towards understanding zebra mussel adhesion.     

Effects of Environmental Factors on Byssal Thread Formation in Some Members of the Family Mytilidae from the Sea of Japan

The ability to attach repeatedly to a substrate (glass, boulders, sand) in three common mussel species of the upper sublittoral zone of the Sea of Japan, Grayan's mussel Crenomytilus grayanus, the Korean mussel Mytilus coruscus, and northern horse mussel Modiolus modiolus, was studied under experimental conditions. It was found that during 120 h of the experiment C. grayanus and M. modiolus produced more byssal threads than M. coruscus. A decrease in the water temperature from 20 to 0°C slowed the rate of production of byssal threads down to full passivity in some experimental mollusks. This was more typical of M. coruscus and less typical of C. grayanus. Renewed threads differed in their length, thick, size of the adhesive plate, and strength. M. coruscus formed the shortest, thickest, and strongest threads with rather a large adhesive disk. The observed differences are discussed from the position of morphophysiological adaptations of species for colonization of different natural substrata under contrasting conditions of the upper sublittoral zone.     

The foot cell morphology of genus Aspergillus

The paper deals with the morphology, development and nature of foot cell in the genusAspergillus. About 69 species belonging to 14 groups have been studied.A. brunneo-uniseriatus (Singh &Bakshi),A. nidulans (Eidam)Wint andAspergillus sp. (ofA. clavatus group) have been selected for detailed developmental studies as they were found to be representative forms of various types of foot cells met within the genus. The foot cell appeared as an enlarged hyphal cell, which, depending upon position of conidiophore became I, L and T shaped but in species ofA. clavatus andA. wentii group it was branched and rhizoidal type due to the development of side protubrances. Effect of different media, pH, sugar concentration and light on foot cell morphology has also been studied. Different media, pH of basal medium and sugar concentration did not show any marked effect on the development and morphology of foot cell while light showed pronounced effect on species ofA. clavatus group.     

Adsorption of chemically synthesized mussel adhesive peptide sequences containing DOPA on stainless steel

The adsorption of proteins at solid–liquid interfaces is important in biosensor and biomaterial applications. Marine mussels affix themselves to surfaces using a highly cross‐linked, protein‐based adhesive containing a high proportion of L‐3,4‐dihydroxyphenylalanine (DOPA) residues. In this work, the effect of DOPA residues on protein adhesion on stainless steel surfaces was studied using a quartz crystal microbalance with dissipation system. The adsorption of two repetitive peptide motifs, KGYKYYGGSS and KGYKYY, from the mussel Mytilus edulis foot protein 5 on stainless steel was studied before and after chemo‐enzymatic modification of tyrosine residues to DOPA using mushroom tyrosinase. Conversion from tyrosine to DOPA, evaluated by HPLC, was in the range 70–99%. DOPA‐modified sequences showed fourfold greater adhesion than unmodified M. edulis foot protein 5 motifs. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.     

d-Alanine metabolism in the lucinid clam Lucinoma aequizonata

The chemoautotrophic symbiont-bearing clam Lucinoma aequizonata contains very high levels of free d-alanine in all tissues. The possible sources for this amino acid and its involvement in the clams' metabolism were investigated. Very low levels of d-alanine (generally below 1 mol·l^-1) were measured in the sediment porewaters from the habitat of the clams. Experiments with ¹⁴C-labeled tracers demonstrate an active metabolism of d-alanine in the clams rather than a role as inert waste product. d-alanine is metabolized at about 0.12 mol·g fw^-1·h^-1. Label from aspartate, but not glucose and CO₂, is incorporated into d-alanine. Incubation with labeled d-alanine did not result in formation of radioactive l-alanine. Tests for alanine racemase (EC 5.1.1.1) and d-amino acid oxidase (EC 1.4.3.3.) did not show activity in either gill, i.e. symbiont and host, or foot tissue. d-Alanine amino transferase (EC 2.6.1.b.) was demonstrated in gill and foot tissues. Two sources for d-alanine are proposed: a degradation of cell walls of symbiotic bacteria and production by the host using a d-specific alanine transaminase.Abbreviations aa amino acid(s) - fw fresh weight - HPLC high-performance liquid chromatography - MBH methyl benzethonium hydroxyde - NAC N-acetyl-l-cysteine - OPA ortho-phthaldialdehyde - TCA tricarbonic acid     

厚壳贻贝Mytilus coruscus足丝盘及足丝的多巴分析

多巴(3,4-1-dihydroxyphenylalanine,DOPA)是贻贝足丝粘附蛋白中的一种特殊的氨基酸,由酪氨酸经羟化后生成,与贻贝足丝粘附蛋白的强粘附性能具有直接联系.目前,已鉴定的多种贻贝足丝蛋白序列中均发现有不同含量的DOPA存在.蛋白中DOPA的定量检测对于了解DOPA在蛋白粘附中的作用以及粘附蛋白的...     

Sperm Ultrastructure of Two Mollusk Species Geukensia demissa and Modiolus modiolus (Mytilidae, Bivalvia)

Sperm ultrastructure was studied in two Atlantic species of bivalve mollusks Geukensia demissa and Modiolus modiolus (Mytilidae). These spermatozoa have a classic structure common for species with external fertilization: the head of the spermatozoon of G. demissa and M. modiolus consists of an acrosome, including an acrosomal vesicle and periacrosomal material, a nucleus, and a middle part with two mutually perpendicular centrioles, surrounded by a ring of spherical mitochondria. The spermatozoa of G. demissa and M. modiolus differ in the general shape and size of the head (M. modiolus, 5.8 × 4 m; G. demissa, 4.2 × 2.5 m), as well as the structure of the acrosome and the number of mitochondria (M. modiolus, 8–12; G. demissa, 5–6). The spermatozoa of the Atlantic species M. modiolus and M. modiolus (M. kurilensis) from the Sea of Japan are close in ultrastructure, but differ in the number of mitochondria. This could possibly be a reason to consider M. modiolus from the Sea of Japan as a separate subspecies, M. modiolus kurilensis. In ultrastructure, the spermatozoa of G. demissa differ significantly from the spermatozoa of M. modiolus, but are similar to the spermatozoa of species of the genus Brachidontes.     

Location and analysis of byssal structural proteins of Mytilus edulis

The acellular attachment organ (byssus) of the marine mussel Mytilus edulis L. is composed of threads that emanate from the body of the mussel to adhesive discs that anchor the threads to rocks, sand and other mussels. Three proteins have been purified by immunohistological methods and located to specific regions of the byssus. A collagenous protein with subunit molecular weights of 53,000, 55,000 and 65,000 is found in the matrix of the elastic thread region. Its 73,000-MW precursor was extracted from foot glands in the area proximal to the animal body and was identified by immune cross-reactivity. A cystine-rich, acidic protein was found in all regions of the byssus associated with a third protein, the polyphenolic protein. The L-dopa-containing polyphenolic protein appears in the cortex of the entire thread and adhesive plaque and at the substrate-plaque interface. Antiserum to this protein stains spherical vesicles in the phenol gland of the foot. Using immuno-electrophoretic methods, the polyphenolic protein and the cystine-rich protein were shown to form high molecular weight aggregates with aging of the byssus.     

Effects of nonnative invertebrates on two life stages of the native eastern oyster <Emphasis Type="Italic">Crassostrea virginica</Emphasis>

Since their recent introductions into Florida waters, three sessile invertebrates [Perna viridis (Asian green mussel), Mytella charruana (charru mussel) and Megabalanus coccopoma (pink titan acorn barnacle)] have expanded their range along the Atlantic coast in estuarine waters. Little research has been done to understand how these nonnative species interact with the ecologically and economically important eastern oyster Crassostrea virginica. To assess the potential effects of P. viridis, M. charruana and M. coccopoma on C. virginica, the following questions were addressed in manipulative experiments. (1) Does the presence of nonnative species decrease oyster larval settlement? (2) Do oyster larvae avoid settling on nonnative species? (3) Do nonnative species decrease survival of juvenile oysters (spat)? (4) Do nonnative species hinder spat growth? We included two controls: absence of nonnative species and presence of the native mussel Geukensia demissa. The nonnative species influenced settlement, growth and survival of C. virginica in different ways. M. coccopoma and P. viridis negatively influenced larval settlement, whereas M. charruana had no influence on the total number of settled larvae. Oyster larvae avoided settling on all three nonnative species and the native G. demissa. Both nonnative mussels negatively affected survival of juvenile oysters but only M. charruana also reduced spat growth. The native mussel, G. demissa, had no negative impacts on total settlement, survival and growth of C. virginica; in fact, it increased larval settlement in some trials. These three nonnative species should be classified as invasive because all had negative effects on native C. virginica.     

The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study

The X-ray crystal structure of lentil lectin in complex with -d-glucopyranose has been determined by molecular replacement and refined to anR-value of 0.20 at 3.0 Å resolution. The glucose interacts with the protein in a manner similar to that found in the mannose complexes of concanavalin A, pea lectin and isolectin I fromLathyrus ochrus. The complex is stabilized by a network of hydrogen bonds involving the carbohydrate oxygens O6, O4, O3 and O5. In addition, the -d-glucopyranose residue makes van der Waals contacts with the protein, involving the phenyl ring of Phe123. The overall structure of lentil lectin, at this resolution, does not differ significantly from the highly refined structures of the uncomplexed lectin.Molecular docking studies were performed with mannose and its 2-O and 3-O-m-nitro-benzyl derivatives to explain their high affinity binding. The interactions of the modelled mannose with lentil lectin agree well with those observed experimentally for the protein-carbohydrate complex. The highly flexible Me-2-O-(m-nitro-benzyl)--d-mannopyranoside and Me-3-O-(m-nitro-benzyl)--d-mannopyranoside become conformationally restricted upon binding to lentil lectin. For best orientations of the two substrates in the combining site, the loss of entropy is accompanied by the formation of a strong hydrogen bond between the nitro group and one amino acid, Gly97 and Asn125, respectively, along with the establishment of van der Waals interactions between the benzyl group and the aromatic amino acids Tyr100 and Trp128.RL and FC are joint first authors.     

Transport of leucine in the cyanobacterium Anabaena variabilis

The amino acid leucine was transported by the cyanobacterium Anabaena variabilis. The K _m for transport was 10.8 M; the V _max was 8.7 nmoles min^–1 mg^–1 chlorophyll a. Transport of leucine was energy dependent: uptake of leucine was inhibited in the dark, and by DCMU and cyanide. Transport was neither dependent on nor enhanced by Na⁺. Prior growth of cells with leucine did not repress transport of [¹⁴C]-leucine. Alanine, glycine, valine, and methionine were strong competitive inhibitors of leucine uptake; serine, threonine, isoleucine, norleucine, and d-alanine competitively inhibited to a lesser degree. Other amino acids or amino acid analogues, including d-leucine, -aminoisobutyrate, and d-serine did not inhibit the transport of leucine.Abbreviations Chl a chlorophyll a - DCMU 3-(3,4-dichlorophenyl)-1,1-dimethylurea - TES N-tris(hydroxymethyl)-2-aminoethane-sulfonic acid - TCA trichloroacetic acid - Tris N-tris(hydroxymethyl)aminoethane     

Spatial distribution of proteins in the quagga mussel adhesive apparatus

The invasive freshwater mollusc Dreissena bugensis (quagga mussel) sticks to underwater surfaces via a proteinacious ‘anchor’ (byssus), consisting of a series of threads linked to adhesive plaques. This adhesion results in the biofouling of crucial underwater industry infrastructure, yet little is known about the proteins responsible for the adhesion. Here the identification of byssal proteins extracted from freshly secreted byssal material is described. Several new byssal proteins were observed by gel electrophoresis. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry was used to characterize proteins in different regions of the byssus, particularly those localized to the adhesive interface. Byssal plaques and threads contain in common a range of low molecular weight proteins, while several proteins with higher mass were observed only in the plaque. At the adhesive interface, a plaque-specific ~8.1 kDa protein had a relative increase in signal intensity compared to the bulk of the plaque, suggesting it may play a direct role in adhesion.     

Mussel glue fromMytilus californianus Conrad: a comparative study

Summary Marine mussels secrete a byssus in order to attach to solid surfaces in the sea. The polyphenolic protein is the glue in the adhesive plaques of the byssus. InMytilus californianus, the polyphenolic protein has an apparent molecular weight of 85,000±5,000 and is rich in the amino acids lysine, 3,4-dihydroxyphenylalanine, serine, threonine, and hydroxyproline. In composition it resembles the polyphenolic protein ofM. edulis (M _r=125,000), although theM. edulis protein contains significantly less isoleucine and more alanine. Tryptic digestion ofM. californianus polyphenolic protein revealed two types of repeating decapeptides (1) (Ser/Thr)-Thr-(Tyr/Dopa)-Hyp-Hyp-Thr-Dopa-Lys-Hyp-Lys and (2) Ile-(Thr/Ser)-(Tyr/Dopa)-Hyp-Hyp-Thr-Dopa-Lys-Hyp-Lys. Residues 2 to 8 are identical with residues 4–10 inM. edulis decapeptides.Abbreviation Dopa 3,4hydroxyphenylalanine     

Selective extraction of CP 26 and CP 29 proteins without affecting the binding of the extrinsic proteins (33, 23 and 17 kDa) and the DCMU sensitivity of a Photosystem II core complex

A highly purified oxygen evolving Photosystem II core complex was isolated from PS II membranes solubilized with the non-ionic detergent n-octyl--D-thioglucoside. The three extrinsic proteins (33, 23 and 17 kDa) were functionally bound to the PS II core complex. Selective extraction of the 22, 10 kDa, CP 26 and CP 29 proteins demonstrated that these species are not involved in the binding of the extrinsic proteins (33, 23 and 17 kDa) or the DCMU sensitivity of the Photosystem II complex.Abbreviations Chl chlorophyll - DCBQ 2,6-dichloro-p-benzoquinone - DCMU 3-(3,4-dichlorophenyl)-1,1-dimethylurea - LHC light-harvesting complex - MES 2-(N-morpholino)ethanesulfonic acid - OGP n-octyl--d-glucoside - OTG n-octyl--d-thioglucoside - PAGE polyacrylamide gel electrophoresis - PS II Photosystem II - SDS sodium dodecyl sulfate     

利用蛋白质组学手段鉴定新型贻贝足丝蛋白

贻贝通过足腺分泌特有的足丝并以此粘附于水下各种基质表面.贻贝足丝中富含各种粘附蛋白,其优异的水下粘附性能使其成为开发新型生物粘合剂的候选分子.厚壳贻贝足丝粘附能力强,本文采用尿素及盐酸胍抽提结合二维双向电泳技术（two-dimensional electrophoresis, 2-DE）,分别对厚壳贻贝足丝纤维和足丝盘的蛋白质进行分离及染色;采用串联质谱技术结合常规搜库和表达序列标签（EST) 数据库搜索,对分离获得的蛋白质点进行鉴定,从中获得了mfp-3、mfp-6、胶原蛋白以及3种未曾报道过的新型贻贝足丝蛋白成分.上述研究为深入了解厚壳贻贝足丝蛋白的分子多样性、探讨其粘附机理以及从中筛选具有应用前景的贻贝足丝蛋白奠定了基础.     

pH-dependent locking of giant mesogens in fibers drawn from mussel byssal collagens

Byssal threads are tough collagenous fibers that mussels use to secure themselves against dislodgement by waves in the marine intertidal zone. Here, preCol, a family of hybrid collagens comprising up to 96% of the protein content in certain regions of byssal threads, was purified in mg amounts from mussel foot tissue for the first time. Conditions for drawing preCols into quality fibers ex vivo were investigated. The most important factor affecting fiber formation was the pH of the drawing solution. The morphology and tensile properties of drawn fibers were also characterized and suggest that a liquid crystal mesophase combined with cross-linking by His-metal coordination plays a role in the assembly/mechanics of drawn fibers and likely in native byssal threads as well.