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Self‐association of the neuroregulatory peptide substance P and its C‐terminal sequences
Author(s) -
Rueger Margitta,
Bienert Michael,
Mehlis Burkhard,
Gast Klaus,
Zirwer Dietrich,
Behlke Joachim
Publication year - 1984
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360230413
Subject(s) - chemistry , peptide , crystallography , stereochemistry , biochemistry
Self‐association of substance P and its C‐terminal partial peptide sequences was studied by CD, quasi‐electric light scattering, and sedimentation experiments. CD spectra of these peptides are strongly influenced by self‐association. They exhibit strong characteristic negative ellipticities, suggesting the formation of a presumably B‐type ordered structure. The tendency to form multimers depends on chain length and constitution and has its maximum at the octapeptide (SP 8). The peptide multimers have a broad distribution of sizes in the range of 30‐ and 800‐nm diameter. Subdivision of this distribution into two size classes gives mean diameters of 60–100 nm (predominating)/200–800 nm for substance P and 30–50 nm/200–800 nm for SP 8 multimers.