24809-25-4Relevant academic research and scientific papers
Discovery of dipeptides with high affinity to the specific binding site for substance P1-7
Fransson, Rebecca,Botros, Milad,Sk?ld, Christian,Nyberg, Fred,Lindeberg, Gunnar,Hallberg, Mathias,Sandstr?m, Anja
supporting information; experimental part, p. 2383 - 2389 (2010/08/22)
Substance P 1-7 (SP1-7, H-Arg-Pro-Lys-Pro-Gln-Gln-Phe-OH) is the major bioactive metabolite of substance P. The interest in this heptapeptide originates from the observation that it modulates, and in certain cases opposes the effects of the parent peptide, e.g., the nociceptive effect. The μ-opioid receptor agonist endomorphin-2 (EM-2, H-Tyr-Pro-Phe-Phe-NH2) has been found to also interact with the specific binding site of SP 1-7 with only a 10-fold lower affinity compared to the native peptide. Considering the smaller size of EM-2 compared to the target heptapeptide, it was selected as a lead compound in the development of low-molecular-weight ligands to the SP1-7 binding site. An alanine scan and truncation study led to the unexpected discovery of the dipeptide H-Phe-Phe-NH2 (Ki = 1.5 nM), having equal affinity as the endogenous heptapeptide SP1-7. Moreover, the studies show that the C-terminal phenylalanine amide is crucial for the affinity of the dipeptide.
Toward an optimal blood-brain barrier shuttle by synthesis and evaluation of peptide libraries
Malakoutikhah, Morteza,Teixidó, Meritxell,Giralt, Ernest
experimental part, p. 4881 - 4889 (2009/08/16)
Several peptide families containing N-methylated amino acids were designed and synthesized using solid-phase peptide synthesis (SPPS). The permeability and phospholipophilicity of these compounds were studied by parallel artificial membrane permeability a
Highly concentrated water-in-oil emulsions as novel reaction media for protease-catalysed kinetically controlled peptide synthesis
Clapes,Espelt,Navarro,Solans
, p. 1394 - 1399 (2007/10/03)
High-internal-phase-ratio-emulsions (HIPREs) or gel emulsions, formulated with a large amount of water (80.0-99.5% w/w), were investigated as reaction media for α-chymotrypsin-catalysed peptide synthesis under kinetic control using Ac-3-Phe-OEt and H-3-Le
Crown ether activation of cross-linked subtilisin Carlsberg crystals in organic solvents
Van Unen, Dirk-Jan,Sakodinskaya, Inna K.,Engbersen, Johan F. J.,Reinhoudt, David N.
, p. 3341 - 3343 (2007/10/03)
The activity of cross-linked subtilisin Carlsberg crystals in the catalysis of peptide bond formation can be significantly enhanced by pretreatment of the enzyme crystals with crown ethers. Soaking of the enzyme crystals in a solution of crown ether in ac
Peptide Synthesis Catalyzed by Modified α-Chymotrypsin in Low-Water Organic Media
Gaertner, H.,Watanabe, T.,Sinisterra, J. V.,Puigserver, A.
, p. 3149 - 3153 (2007/10/02)
Enzyme-catalyzed synthesis of peptide bonds in organic solvents has been investigated by using α-chymotrypsin either modified with poly(ethylene glycol) or immobilized on different supports, in order to find out the importance of water content in the reaction.High yields of peptide synthesis were obtained whatever the type of enzyme derivative used.By varying the type of support, a modification in the enzyme environment was observed and resulted in a significant increase in the reaction yield when nucleophiles with poor affinity for the enzyme were used.Since organic solvents also affected substrate specificity with respect to the donor ester, a general methodology was proposed for the enzymatic synthesis of peptides in low-water organic media.
