Role of arginine in chemical cross-linking with N-hydroxysuccinimide esters.
In order to clarify whether arginine has a promoting effect on the acylation of hydroxyl groups of serine, threonine, or tyrosine by homobifunctional cross-linking agents in aqueous solution, we carried out systematic experiments with model peptides, comparing relative reaction yields with covalently protected and unprotected arginines by MALDI-MS. The guanidinium group could be demonstrated to contribute to the reactivity of hydroxyl groups toward N-hydroxysuccinimide esters and catalyze the nucleophilic substitution, probably via hydrogen bonds.
Mädler
Stefanie
S
Department of Chemistry and Applied Biosciences, ETH Zurich, CH-8093 Zurich, Switzerland.
Gschwind
Sabrina
S
Zenobi
Renato
R
D000215:Acylation; D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry* / Q000502:physiology; D003432:Cross-Linking Reagents / Q000737:chemistry*; D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013388:Succinimides / Q000737:chemistry*
D003432:Cross-Linking Reagents; D010455:Peptides; D013388:Succinimides; D001120:Arginine; C001426:N-hydroxysuccinimide