Non-covalent interactions between proteins and polysaccharides

Foods with novel or improved properties can be created by utilizing non-covalent interactions between proteins and polysaccharides. In solution, either attractive or repulsive interactions between proteins and polysaccharides can be used to create microstructures that give foods novel textural and sensory properties. At interfaces, attractive electrostatic interactions can be used to create food emulsions with improved stability to environmental stresses or with novel encapsulation-release characteristics.     

Interaction between acidic polysaccharides and proteins

There was an ionic interaction between acidic polysaccharides (APS) and proteins at the pH range in which APS were negatively charged and proteins were positively charged, and in enzymes the interaction was detected as a change in the enzyme activity. At pH 4.7, acid phosphatase (pI, 5.4), alpha-glucosidase (pI, 5.7), and beta-glucosidase (pI, 7.3) were inhibited by APS to various extents. On the other hand, alpha-glucosidase and alkaline phosphatase (pI, 4.5) were not inhibited by APS at pH 6.8 and 9.8, respectively, most of these two enzymes being negatively charged at the respective pHs. Sulfated polysaccharides combined with hemoglobin (pI, 6.8 to approximately 7.0) by an ionic bond at pH 2 to make hemoglobin unsusceptible to proteolysis by pepsin, but polyuronides which were not charged at this pH did not affect hydrolysis of hemoglobin.     

Cross-reactions between human and animal plasma proteins

Summary The rôle of several structural and functional factors and of concentration on the cross-reactions of 28 human plasma proteins with their homologues in animal blood was investigated. The Immunological Evolution Group (IEG) system was employed for this purpose as described earlier (Bauer, 1970 a). No interaction of structural factors was detected, while an influence of serum level of the different proteins could not be ruled out with certainty.At least in the case of the 4 immunoglobulins and the 3 complement factors, included in the IEG-system, protein function and evolution show some degree of correlation, indicating the influence of function on molecular evolution in the case of these plasma proteins.     

Cross-reactions between human and animal plasma proteins

Summary Cross-reactions between human plasma proteins and their homologues in primate blood were investigated systematically. From the three groups of proteins distinguished earlier [2] two have been especially examined; these findings are reported and discussed in the present communication. The Immunological Evolution Group (IEG) I, comprising IgA (-chain), IgD (-chain) and inter--trypsininhibitor, cross-reacts with pongid plasma only, IEG IIa, i.e. IgM (-chain), ₂-glycoproteins II and III and cholinesterase, does so with the pongid and cercopithecoid plasmas tested; IEG IIb, including acid _l-glycoprotein, _2HS-glycoprotein, _l-trypsininhibitor, haptoglobin and hemopexin, cross-reacts with pongid, cercopithecoid and cebus (platyrrhinian) plasma and finally IEG IIc, consisting of transferrin and Gc-globulin, does so with all primate plasmas tested, including prosimians. All the proteins named do not cross-react however with non-primate proteins as do those of IEG III. It is concluded, that the determinants reacting in the primate proteins increase in their evolutionary ages from IEG I over IEG IIa, IIb to IIc in the same way as the last common ancestors of man and the crossreacting species increase.

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Zusammenfassung Die Kreuzreaktionen zwischen menschlichen Plasmaeiweißen und ihren Homologen im Blut von subhumanen Primaten wurden systematisch untersucht. Von den drei früher voneinander abgetrennten Gruppen [2] wurden zwei für die vorliegende Versuchsreihe herausgegriffen; eine von ihnen konnte weiter unterteilt werden. Die erhobenen Befunde werden berichtet und diskutiert. Die Immunologische Evolutions-Gruppe (IEG) I, die IgA (-Kette), IgD (-Kette) und den Inter--Trypsininhibitor umfaßt, zeight Kreuzreaktionen nur mit den Plasmen von Pongiden. Die IEG IIa, zu der IgM (-Kette), die ₂ II und III und Cholinesterase gehören, kreuzreagiert mit den entsprechenden Plasmaproteinen der geprüften Pongiden und Cercopithecoidea, die IEG IIb—das sind saueres _l-Glycoprotein, _2HS-Glycoprotein, _l-Trypsininhibitor, Haptoglobin und Haemopexin — mit Pongiden, Cercopithecoidea und Cebus (Platyrrhini) und endlich die IEG IIc, die sich aus Transferrin und dem Gc-Globulin zusammensetzt, mit allen geprüften Primatenplasmen einschließlich denen von Prosimiern. Alle hier genannten Plasmaeiweiße zeigen jedoch keine Kreuzreaktionen mit Proteinen von Nichtprimaten, wie dies bei der IEG III der Fall ist.Aus den vorliegenden Befunden wird der Schluß gezogen, daß die Determinanten der Primatenproteine, die jeweils reagieren, in ihrem phylogenetischen Alter von IEG Iüber IEG IIa, IIb, IIc im gleichen Maße ansteigen, wie die letzten gemeinsamen Vorfahren von Mensch und den kreuzreagierenden Arten.

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(Chief: Prof. Dr. E. Krah)     

Density discriminates between thermophilic and mesophilic proteins

Despite an intense interest and a remarkable number of studies on the subject, the relationships between thermostability and (primary, secondary and tertiary) structure of proteins are still not fully understood. Here, comparing the protein density – defined by the ratio between the residue number and protein excluded volume – for a set of thermophilic/mesophilic pairs, we provide evidence that this property is connected to the optimal growth temperature. In particular, our results indicate that thermophilic proteins have – in general – a lower density with respect to the mesophilic counterparts, being such a correlation more pronounced for optimal growth temperature differences greater than 40°C. The effect of the protein thermostability changes on the molecular shape is also presented.     

Interaction between proteins and cationic gemini surfactant

Surface tension, fluorescence, and circular dichroism (CD) methods have been used to investigate the interaction between cationic gemini surfactant 1,2-ethane bis(dimethyldodecylammonium bromide) (C12C2C12) and proteins including bovine serum albumin (BSA) and gelatin. Surface tension measurements show that the complexes of gelatin--C12C2C12 form more easily than that of BSA--C12C2C12. Addition of C12C2C12 has a different effect not only on the polarity of the microenvironment in BSA and gelatin systems but also on their fluorescence spectra. It can be seen from far-UV CD spectra that the alpha-helical network of BSA is disrupted and its content decreases from 41.7% to 27.6% while the random coil content of gelatin increases from 53.0% to 55.9% with increasing C12C2C12 concentration. The results from near-UV CD spectra show that the binding of C12C2C12 induces changes of the microenvironment around the aromatic amino acid residues and disulfide bonds of BSA at high C12C2C12 concentrations.     

Interactions between GPI-anchored proteins and membrane lipids

Proteins anchored in membranes by glycosylphosphatidylinositol (GPI) are widely distributed, but the function of this unusual anchor is a puzzle. Recent evidence shows that these proteins can associate with membrane lipids in special ways. One function of GPI anchorage may be to allow proteins to interact with specialized membrane domains.     

Electron transfer between heme proteins and ceruloplasmin

Reduced cytochrome-c, reduced myoglobin and oxyhemoglobin respectively have been oxidized to oxidized cytochrome-c, metmyoglobin and methemoglobin by ceruloplasmin. Metmyoglobin and methemoglobin formation was stoichiometric while oxidized cytochrome-c reacted catalytically. Only 50% methemoglobin was formed which suggested that two hemes out of four could transfer electrons. Hydrogen peroxide was formed in the reaction of reduced cytochrome-c with ceruloplasmin.     

Interactions between neurotensin receptors and G proteins

Three neurotensin (NT) receptors have been cloned to date, two of which, NTS1 and NTS2, belong to the family of seven transmembrane domain receptors coupled to G proteins (GPCRs). NTS1 and NTS2 may activate multiple signal transduction pathways, involving several G proteins. However, whereas NT acts as an agonist towards all NTS1-mediated pathways, this peptide may exert either agonist or antagonist activities, depending on the NTS2-mediated pathway in question. Studies on these receptors reinforce the concept of independence between multiple signals potentially mediated through a single GPCR, generating a wide diversity of functional responses depending on the host cell and the ligand.     

Decipher the connections between proteins and phenotypes

As the outward-most representation of life, phenotype is the fundamental basis with which humans understand life and disease. But with the advent of molecular and sequencing technique and research, a growing portion of science research focuses primarily on the molecular level of life. Our understanding in molecular variations and mechanisms can only be fully utilized when they are translated into the phenotypic level. In this study, we constructed similarity network for phenotype ontology, and then applied network analysis methods to discover phenotype/disease clusters. Then, we used machine learning models to predict protein-phenotype associations. Each protein was characterized by the functional profiles of its interaction neighbors on the protein-protein interaction network. Our methods can not only predict protein-phenotype associations, but also reveal the underlying mechanisms from protein to phenotype.