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Controlled micelle conjugation via charged peptide amphiphiles
Author(s) -
Truong Thien Van,
Ghosh Mihir,
Hosamani Basavaprabhu,
Baiju Thekke V.,
Dhandapani Gunasekaran,
Wachtel Ellen,
Kesselman Ellina,
Danino Dganit,
Sheves Mordechai,
Namboothiri Irishi N.N.,
Patchornik Guy
Publication year - 2019
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.3174
Subject(s) - amphiphile , micelle , peptide , chemistry , conjugated system , absorption (acoustics) , membrane , combinatorial chemistry , biophysics , organic chemistry , biochemistry , materials science , copolymer , aqueous solution , polymer , biology , composite material
We report the first demonstration of nonionic detergent micelle conjugation and phase separation using purpose‐synthesized, peptide amphiphiles, C 10 ‐(Asp) 5 and C 10 ‐(Lys) 5 . Clustering is achieved in two different ways. Micelles containing the negatively charged peptide amphiphile C 10 ‐(Asp) 5 are conjugated (a) via a water‐soluble, penta‐Lys mediator or (b) to micelles containing the C 10 ‐(Lys) 5 peptide amphiphile. Both routes lead to phase separation in the form of oil‐rich globules visible in the light microscope. The hydrophobic nature of these regions leads to spontaneous partitioning of hydrophobic dyes into globules that were found to be stable for weeks to months. Extension of the conjugation mechanism to micelles containing a recently discovered, light‐driven proton pump King Sejong 1‐2 (KS1‐2) demonstrates that a membrane protein may be concentrated using peptide amphiphiles while preserving its native conformation as determined by characteristic UV absorption. The potential utility of these peptide amphiphiles for biophysical and biomedical applications is discussed.