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Switch Peptides: pH‐Induced α‐Helix to β‐Sheet Transitions of Bis‐amphiphilic Oligopeptides
Author(s) -
Mutter Manfred,
Gassmann R.,
Buttkus U.,
Altmann K.H.
Publication year - 1991
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199115141
Subject(s) - amphiphile , helix (gastropod) , aqueous solution , chemistry , oligopeptide , protein secondary structure , solvent , beta sheet , conformational change , peptide , crystallography , stereochemistry , biophysics , biochemistry , organic chemistry , polymer , copolymer , biology , ecology , snail
The interconversion of two secondary structure types (α‐helix ⇆ β‐sheet) induced by external conditions such as pH, temperature, concentration, and solvent could be proved in a new class of amphiphilic peptides (switch peptides) in aqueous solution. The pH‐dependent conformational changes were studied by CD spectroscopy. Special attention was given to the investigations of four newly synthesized peptides with similar sequences.