Effects of conformational stability and geometry of guanidinium display on cell entry by beta-peptides.
We have used our ability to control beta-peptide secondary structure in order to explore the effects of conformational stability and geometry of guanidinium display on cell entry. Both of these factors affect the rate and relative amount of beta-peptide accumulation in the cytoplasm and nucleus of live HeLa cells. These beta-peptides do not show significant differences in cell surface binding, implying that structure and guanidinium display are important in a later step in cell entry than initial surface binding.
Potocky
Terra B
TB
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Menon
Anant K
AK
Gellman
Samuel H
SH
D001120:Arginine / Q000737:chemistry* / Q000378:metabolism*; D004705:Endocytosis; D019791:Guanidine / Q000737:chemistry* / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D001120:Arginine; D019791:Guanidine