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Synthesis and conformational analysis of salivary proline-rich peptide P-B

✍ Scribed by Elżbieta Kamysz; Emilia Sikorska

Book ID
105359926
Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
349 KB
Volume
16
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

The 57‐amino acid human salivary polypeptide P‐B has been synthesized by the solid‐phase method using 9‐fluorenylmethoxycarbonyl (Fmoc) strategy. The circular dichroism (CD) spectroscopy, Fourier‐transform infrared spectroscopy (FTIR) and molecular modeling methods have been used for conformational studies of P‐B. Examination of the CD spectra of P‐B showed the content of the secondary structure to be independent of temperature over the range 0–60 °C at pH = 7 as well as over the pH range of 2–12 at 37 °C. P‐B adopts predominantly unordered structure with locally appearing β‐turns. The cumulative results obtained using the CD and FTIR spectroscopic techniques indicate the percentage of the polyproline type‐II (PPII) helix being as low as about 10%. Similarly, the molecular dynamics (MD) simulations reveal only a short PPII helix in the C‐terminal fragment of the peptide (Pro^51^–Pro^54^), which constitutes 7%. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.

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