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Identification of peptide hormones of the amphipathic helix class using the helical hydrophobic moment algorithm
Author(s) -
Dohlman Jan G.,
De Loof Hans,
Prabhakaran M.,
Koopman William J.,
Segrest Jere P.
Publication year - 1989
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340060106
Subject(s) - amphiphile , peptide , residue (chemistry) , helix (gastropod) , chemistry , sequence (biology) , biochemistry , biology , organic chemistry , copolymer , ecology , snail , polymer
Eisenberg's helical hydrophobic moment (<μ H >) algorithm was applied to the analysis of the primary structure of amphipathic α‐helical peptide hormones and an optimal method for identifying other peptides of this class determined. We quantitate and compare known amphipathic helical peptide hormones with a second group of peptides with proven nonamphipathic properties and determine the best method of distinguishing between them. The respective means of the maximum 11 residue <μ H > for the amphipathic helical and control peptides were 0.46 (±/−0.07) and 0.33 (0.07) ( P +0.004). To better reflect the amphipathic potential of the entire peptide, the percent of 11 residue segments in each peptide above a particular <μ H > was plotted vs <μ H >. The resulting curves are referred to as HM‐C. The mean HM‐C (of the two groups) was highly significantly different such that the HM‐C method was superior to others in its ability to distinguish amphipathic from nonamphipathic peptides. Several potential new members of this structural class were identified using this approach. Molecular modeling of a portion of one of these, prolactin inhibitory factor, reveals a strongly amphipathic α helix at residues 4–21. This computer‐based method may enable rapid identification of peptide of the amphipathic α‐helix class.