Abstract：
:Dynamic light scattering measurements were carried out on secretin in aqueous solution (2 mM; pH 5.0). The results indicated that the molecule exists as a fairly compact hexamer under these solution conditions. Secondary structural properties of the secretin hexameric complex were evaluated using CD and NMR spectroscopy. Specifically, the spectral properties of secretin in water were examined as a function of peptide concentration. Results from the analyses indicated a 2-fold increase (17-32%) in alpha-helical content within the region Ser11-Arg21 as the peptide concentration was increased from 0.1 to 2 mM. Displacement of the alphaH proton chemical shifts relative to random coil values did not alter significantly with increasing peptide concentration. This observation confirmed that the length of the helical segment is independent of peptide concentration between 0.1 and 2 mM. The nature of the helix was furthermore determined as amphipathic, and thus the potential for a cooperative intermolecular association through the apolar helical face of individual monomers was indicated. These findings suggest that secretin aggregates into symmetric hexamers at millimolar concentrations and, furthermore, that the helical domain is stabilized through this intermolecular association. The potential for secretin to bind divalent cations, including Ca2+ and Zn2+, was also examined by CD1 and NMR spectroscopy. The results revealed that Zn2+ specifically coordinates to the His1 and Asp3 residues of each secretin monomer without disrupting the peptide's helical structure, whereas Ca2+ did not exhibit any interaction with the peptide hormone. It was concluded from these studies that secretin may be stored in a hexameric form within its secretory tissues and that zinc may play a role in the storage of secretin through a specific interaction with the N-terminal histidine and aspartic acid residues.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Carpenter KA,Schiller PWdoi
10.1021/bi980701xsubject
Has Abstractpub_date
1998-12-01 00:00:00pages
16967-74issue
48eissn
0006-2960issn
1520-4995pii
bi980701xjournal_volume
37pub_type
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