Self-association of Na-protected peptides related to Cterminal sequences of substance P in methylene chloride was disrupted by adding increasing amounts of various polar organic solvents. This process was monitored by the disappearance of the amide I C=O stretching band (1630 cm-I ) of strongly inte
Self-association of the neuroregulatory peptide substance P and its C-terminal sequences
✍ Scribed by Margitta Rueger; Michael Bienert; Burkhard Mehlis; Klaus Gast; Dietrich Zirwer; Joachim Behlke
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1984
- Tongue
- English
- Weight
- 584 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
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.
📜 SIMILAR VOLUMES
We describe the construction of a compact protein sequencer designed specifically for the C-terminal sequence analysis of peptides and proteins. This sequencer has a vertical flow path and is equipped with a continuous flow reactor (CFR). The flow paths for the various reagents and solvents have bee