A computergraphic determination of the chemotactic peptide preferred conformation |
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Authors: | S F Semus E L Becker C Toniolo R J Freer |
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Institution: | Department of Pharmacology, Medical College of Virginia, Richmond 23298. |
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Abstract: | Replacement of leucine in the chemotactic peptide For-Met-Leu-Phe by the sterically constrained amino acids alpha-aminoisobutyric acid and aminocyclohexanecarboxylic acid affords compounds of equal or greater activity than the parent. NMR studies indicate that the parent compound is present as a beta-sheet in solution, whereas the analogues prefer a beta-turn. Application of molecular modelling would indicate that the beta-turn conformer is energetically preferable and thus suggests that it is the orientation adopted by the peptides. |
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