Conformation of human calcitonin gene-related peptide (8-37) in aqueous solution as determined by circular dichroism spectroscopy.
Circular dichroism (CD) studies on CGRP(8-37) indicate that there is some latent alpha-helical structure in aqueous solution. However, the amount is quite small (approximately 10% at 5 degrees C), which is substantially less than for CGRP itself (approximately 15-20%). Upon addition of helix-promoting materials, such as trifluoroethanol and sodium dodecyl sulphate, the helix content increases dramatically. No evidence for helix stabilization upon the addition of zinc was observed.
Matsuura
J
J
School of Pharmacy, University of Colorado Health Sciences Center, Denver 80262.
Manning
M C
MC
D001665:Binding Sites; D002116:Calcitonin; D015740:Calcitonin Gene-Related Peptide / Q000737:chemistry*; D002942:Circular Dichroism; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary / Q000187:drug effects; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D012996:Solutions; D014270:Trifluoroethanol / Q000494:pharmacology; D014867:Water; D015032:Zinc / Q000378:metabolism
D010446:Peptide Fragments; D012996:Solutions; D014867:Water; C058636:calcitonin gene-related peptide (8-37); D012967:Sodium Dodecyl Sulfate; D014270:Trifluoroethanol; D002116:Calcitonin; D015032:Zinc; D015740:Calcitonin Gene-Related Peptide