Premium
Synthesis and conformational analysis of salivary proline‐rich peptide P‐B
Author(s) -
Kamysz Elżbieta,
Sikorska Emilia
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1297
Subject(s) - polyproline helix , circular dichroism , chemistry , peptide , fourier transform infrared spectroscopy , protein secondary structure , helix (gastropod) , proline , crystallography , amino acid , vibrational circular dichroism , stereochemistry , infrared spectroscopy , biochemistry , organic chemistry , biology , ecology , physics , quantum mechanics , snail
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.