Metal-assisted assembly and stabilization of collagen-like triple helices.
Single-chain and TRIS-assembled collagen mimetic peptide structures incorporating catechol groups were synthesized. When 1/3 equiv of Fe3+ was added to the single-chain compound in 50 mM CAPS buffer (pH 10), the 1:3 Fe3+-catechol complex that formed acted as an N-terminal scaffold to assemble the triple helix. When 1 equiv of Fe3+ was added to the TRIS-assembled compound in the buffer solution, the Fe3+-catechol complex acted as an extra C-terminal scaffold, which lead to a triple helix with both termini tethered. The formation of this C-terminal complex increased the Tm by a remarkable 22 degrees C!
Cai
Weibo
W
Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, California 92093, USA.
Kwok
Sen Wai
SW
Taulane
Joseph P
JP
Goodman
Murray
M
D002396:Catechols / Q000737:chemistry*; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D005290:Ferric Compounds / Q000737:chemistry*; D007502:Iron Chelating Agents / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet; D014325:Tromethamine / Q000737:chemistry
D002396:Catechols; D005290:Ferric Compounds; D007502:Iron Chelating Agents; D010455:Peptides; D014325:Tromethamine; D003094:Collagen