Wiley
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Synthesis and biological activity of Substance P <i>C</i>‐terminal hexapeptide and heptapeptide analogues The analogues [Glu(OBzl)11 ]SP6–11 and [Glu(OBzl)11 ]SP5–11 of the C‐terminal hexapeptide and heptapeptide of Substance P have been synthesized by conventional solution methods. In each analogue the SCH3 group of Met11 is replaced by the COOCH2 C6 H5 group. The in vitro activity of both analogues has been determined on three biological preparations: guinea pig ileum (GPI), rat vas deferens (RVD), and rat portal vein (RPV). The selectivity for the different receptors has been studied by utilizing atropine‐treated guinea pig ileum (GPI + At). The results showed that both analogues are mainly active on GPI through the NK‐1 receptor and that both analogues are equipotent to Substance P.
Tập 37 Số 3 - Trang 180-184 - 1991
Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acids 9‐Fluorenylmethoxycarbonyl (Fmoc) amino acids were first used for solid phase peptide synthesis a little more than a decade ago. Since that time, Fmoc solid phase peptide synthesis methodology has been greatly enhanced by the introduction of a variety of solid supports, linkages, and side chain protecting groups, as well as by increased understanding of solvation conditions. These advances have led to many impressive syntheses, such as those of biologically active and isotopically labeled peptides and small proteins. The great variety of conditions under which Fmoc solid phase peptide synthesis may be carried out represents a truly “orthogonal” scheme, and thus offers many unique opportunities for bioorganic chemistry.
Tập 35 Số 3 - Trang 161-214 - 1990
Amino acid structure and “difficult sequences” in solid phase peptide synthesis Deprotection peak profiles have been determined as a measure of internal aggregation during Fmoc‐polyamide continuous flow solid phase synthesis. The results have been correlated with amino‐acid structure and discussed in terms of minimising aggregation during synthesis.
Tập 40 Số 3-4 - Trang 300-307 - 1992
Semisynthesis of carboxy‐terminal fragments of thermolysin Enzyme‐catalyzed synthesis of two polypeptide fragments, one of which is obtained by chemical synthesis, in the presence of proteolytic enzymes and in aqueous organic solvents constitutes a convenient procedure for the synthesis of proteins and their analogs. This novel semisynthetic procedure was investigated for preparingCOOH ‐terminal fragments of the metallo‐protease thermolysin. Fragment 205–316, obtained by autolysis of the protein in the presence of EDTA, was first cleaved selectively withStaphylococcus aureus V8 protease at the level of the single Glu302 residue into fragments 205–302 and 303–316. Upon incubation for 2–5 days of fragment 205–302 with a 5–fold excess of peptide 303–316, prepared by solid phase synthesis, with V8‐protease in 0.1M ammonium acetate, pH6.0, containing 50% glycerol as organic cosolvent, enzyme‐catalyzed reformation of the peptide bond was achieved in yields up to ñ90% (based on fragment 205–302). The same procedure was used to prepare also the thermolysin fragments 205–315 and 205–311 by enzymatic coupling of fragment 205–302 to peptide 303–315 or 303–311, these last prepared by proteolytic digestion of the synthetic peptide 303–316. This procedure of semisynthesis opens up an approach for the site‐directed modification of the tetrahelicalCOOH ‐terminal fragment 205–316 of thermolysin at the level of its helical segment encompassing residues 301–312 in the native, intact protein. Such analogs will be useful for examining structure‐folding‐stability relationships in this folded fragment possessing domain‐like characteristics.
Tập 35 Số 3 - Trang 219-221 - 1990