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A Solid Phase Vibrational Circular Dichroism Study of Polypeptide–Surfactant Interaction
Author(s) -
Novotná Pavlína,
Urbanová Marie
Publication year - 2015
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.22534
Subject(s) - circular dichroism , chemistry , chirality (physics) , sodium dodecyl sulfate , vibrational circular dichroism , crystallography , pulmonary surfactant , helix (gastropod) , glutamic acid , protein secondary structure , amino acid , stereochemistry , organic chemistry , biochemistry , ecology , chiral symmetry breaking , physics , quantum mechanics , snail , nambu–jona lasinio model , biology , quark
We studied the interaction of poly‐ l ‐lysine (PLL) and poly‐ l ‐arginine (PLAG) with sodium dodecyl sulfate (SDS) surfactant and the interaction of poly‐ l‐ glutamic acid (PLGA) and poly‐ l ‐aspartic acid (PLAA) with tetradecyltrimethylammonium bromide (TTAB) surfactant using vibrational circular dichroism (VCD) spectroscopy in the region of C‐H stretching vibration and in the Amide I region both in solution and in mulls. A chirality transfer from polypeptides to achiral surfactants was observed in the C‐H stretching region, where measurements in solution were impossible. This observation was enabled by a special sample treatment technique using lyophilization and the preparation of mulls. This technique demonstrated itself as an interesting and beneficial tool for VCD measurements. In addition, we observed that SDS changed the secondary structure of PLL to the β‐sheet and of PLAG to the α‐helix. TTAB disrupted the PLGA and PLAA structure. These results were obtained in the mull but were confirmed by the VCD spectra measured in solution and by electronic circular dichroism. The chirality transfer from the polypeptides to SDS was caused by polypeptides ordered into a specific conformation during the interaction, while in the TTBA system it was induced primarily by the chirality of the amino acid residues. Chirality 27:965–972, 2015 . © 2015 Wiley Periodicals, Inc.