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Curvature sensing MARCKS‐ED peptides bind to membranes in a stereo‐independent manner
Author(s) -
Yan Lei,
Jesus Armando Jerome,
Tamura Ryo,
Li Victoria,
Cheng Kui,
Yin Hang
Publication year - 2015
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.2772
Subject(s) - marcks , membrane curvature , membrane , peptide , chemistry , biophysics , myristoylation , curvature , lipid bilayer , biology , biochemistry , geometry , mathematics
Membrane curvature and lipid composition plays a critical role in interchanging of matter and energy in cells. Peptide curvature sensors are known to activate signaling pathways and promote molecular transport across cell membranes. Recently, the 25‐mer MARCKS‐ED peptide, which is derived from the effector domain of the myristoylated alanine‐rich C kinase substrate protein, has been reported to selectively recognize highly curved membrane surfaces. Our previous studies indicated that the naturally occurring l ‐MARCKS‐ED peptide could simultaneously detect both phosphatidylserine and curvature. Here, we demonstrate that d ‐MARCKS‐ED, composed by unnatural d ‐amino acids, has the same activities as its enantiomer, l ‐MARCKS‐ED, as a curvature and lipid sensor. An atomistic molecular dynamics simulation suggests that d ‐MARCKS‐ED may change from linear to a boat conformation upon binding to the membrane. Comparable enhancement of fluorescence intensity was observed between d ‐ and l ‐MARCKS‐ED peptides, indicating similar binding affinities. Meanwhile, circular dichroism spectra of d ‐ and l ‐MARCKS‐ED are almost symmetrical both in the presence and absence of liposomes. These results suggest similar behavior of artificial d ‐ and natural l ‐MARCKS‐ED peptides when binding to curved membranes. Our studies may contribute to further understanding of how MARCKS‐ED senses membrane curvature as well as provide a new direction to develop novel membrane curvature probes. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.