Catalytic unfolding and proteolysis of cytochrome C induced by synthetic binding agents.
A class of polyanionic copper porphyrin dimers is shown to selectively increase the susceptibility of cytochrome c to proteolysis through binding-induced disruption of tertiary and secondary structure. The free energy of the protein conformation leading to proteolytic attack is stabilized by about 2.4 kcal/mol in the bound state. The proteolytic acceleration is catalytic in nature, requiring only a fraction of an equivalent of metalloporphyrin to effect complete, rapid digestion in the presence of a protease.
Contribution from the Department of Chemistry, Yale University, New Haven, CT 06511, USA.
Kevin
K
Groves
Andrew J
AJ
Wilson
Andrew D
AD
Hamilton
D000595:Amino Acid Sequence; D002384:Catalysis; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry; D045304:Cytochromes c / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D008665:Metalloporphyrins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013056:Spectrophotometry, Ultraviolet; D014357:Trypsin / Q000737:chemistry
D008665:Metalloporphyrins; D003300:Copper; D045304:Cytochromes c; D014357:Trypsin