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.
School of Pharmacy, University of Colorado Health Sciences Center, Denver 80262.
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J
Matsuura
M C
MC
Manning
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