H-Arg-Arg-OH is a basic dipeptide composed of two arginine molecules linked by a peptide bond[1]. Under physiological conditions, H-Arg-Arg-OH carries a strong positive charge, possesses excellent water solubility, and has specific enzymatic cleavage sites[2]. H-Arg-Arg-OH is a classic specific substrate for serine proteases such as trypsin and is commonly used in enzyme kinetics studies and enzyme activity assays. Its strong basic characteristics also make it a model molecule for studying the interaction between cationic peptides and biological membranes[2]. H-Arg-Arg-OH is suitable for biochemical research, enzymatic experiments, and as an intermediate or reference standard in polypeptide synthesis[3, 4].
References:
[1] Atkinson C E, Aliev A E, Motherwell W B. Binding site optimisation for artificial enzymes by diffusion NMR of small molecules[J]. Chemistry–A European Journal, 2003, 9(8): 1714-1723.
[2] Smiljanic E. Some studies of artificial enzyme systems[M]. University of London, University College London (United Kingdom), 2006.
[3] Lee Y, Yang J, Rudich S M, et al. Improved planar amperometric nitric oxide sensor based on platinized platinum anode. 2. Direct real-time measurement of NO generated from porcine kidney slices in the presence of L-arginine, L-arginine polymers, and protamine[J]. Analytical chemistry, 2004, 76(3): 545-551.
[4] Arendt M, Sun W, Thomann J, et al. Dendrimeric bisphosphonates for multivalent protein surface binding[J]. Chemistry–An Asian Journal, 2006, 1(4): 544-554.