TY - JOUR
T1 - Comparison of the binding of α-helical and β-sheet peptides to a hydrophobic surface
AU - Steer, David L.
AU - Thompson, Philip E.
AU - Blondelle, Sylvie E.
AU - Houghten, Richard A.
AU - Aguilar, Marie Isabel
PY - 1998/6/8
Y1 - 1998/6/8
N2 - The induction and stabilisation of secondary structure for a series of amphipathic α-helical and β-sheet peptides upon their binding to lipid- like surfaces has been characterised by reversed phase high-performance liquid chromatography (RP-HPLC). In addition, a series of peptides which have been shown to switch from β-sheet to α-helical conformation upon transfer from a polar to a non-polar solution environment also have been studied. Binding parameters related to the hydrophobic contact area and affinity for immobilised C18 chains were determined at temperatures that ranged from 5 to 85°C, allowing conformational transitions for the peptides during surface adsorption to be monitored. The results demonstrated that all peptides which adopt secondary structure in solution also exhibited large changes in their interactive properties. Overall, this study demonstrates that the hydrophobic face of each amphipathic peptide dominates the binding process and that hydrophobic interactions are a major factor controlling the surface induction of secondary structure.
AB - The induction and stabilisation of secondary structure for a series of amphipathic α-helical and β-sheet peptides upon their binding to lipid- like surfaces has been characterised by reversed phase high-performance liquid chromatography (RP-HPLC). In addition, a series of peptides which have been shown to switch from β-sheet to α-helical conformation upon transfer from a polar to a non-polar solution environment also have been studied. Binding parameters related to the hydrophobic contact area and affinity for immobilised C18 chains were determined at temperatures that ranged from 5 to 85°C, allowing conformational transitions for the peptides during surface adsorption to be monitored. The results demonstrated that all peptides which adopt secondary structure in solution also exhibited large changes in their interactive properties. Overall, this study demonstrates that the hydrophobic face of each amphipathic peptide dominates the binding process and that hydrophobic interactions are a major factor controlling the surface induction of secondary structure.
KW - α-helix
KW - β-sheet
KW - Amphipathicity
KW - Binding affinity
KW - Hydrophobic contact area
KW - RP-HPLC
UR - http://www.scopus.com/inward/record.url?scp=0031779742&partnerID=8YFLogxK
M3 - Article
C2 - 9650714
SN - 1399-3011
VL - 51
SP - 401
EP - 412
JO - Journal of Peptide Research
JF - Journal of Peptide Research
IS - 6
ER -