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ENZYMATIC PEPTIDE SYNTHESIS Fred Widmer*, Motonori Ohno, Mark Smith, Nancy Nelson and Christian B. Anfinsen Laboratory of Chemical Biology, NIH, Bethesda, Maryland, USA Introduction The possibility that hydrolytic enzymes should in principle be applicable to catalyze a process in the reverse, i.e. the syn- thetic direction, was already pointed out by van't Hoff in 1898 (1). For proteolytic enzymes, recently intensified efforts by several groups to utilize this potential for practical purposes in preparative peptide synthesis have met with considerable su

CONTINUOUS FLOW PEPTIDE SYNTHESIS R. Frank, H.Gausepohl European Molecular Biology Laboratory, Heidelberg Introduction The introduction of solid phase peptide synthesis by R.B. Merrifield in 1962 (1) induced tremendous activity in peptide synthesis. A large number of biologically active peptides have been synthesized using reaction conditions close to Merrifield's original version. The repetitive nature of the operations in the solid phase concept soon led to the development of several automated instruments (2, 3), for the assembly of peptide chains

Synthese und katalytische Eigenschaften hydrolytisch aktiver Peptide Synthesis and Catalytic Properties of Peptides with Hydrolytic Activity Dorothee Petz und Friedhelm Schneider Physiologisch-Chemisches Institut II, Universität Marburg (Z. Naturforsch. 31c, 534 — 543 [1976]; eingegangen am 24. Juni 1976) Peptide Synthesis, Peptides with Hydrolytic Activity The synthesis by conventional methods of the peptides Z-Asp-Cys-NH2, Z-Asp-Gly-Cys-NH2 , Z-Glu-Gly-Cys-NH2, Z-His-Ala-Gly-Gly-Cys-NH2, Z-His-Ala-Asp-Gly-Cys-NH2 and Z-His-Ala-Asp- Gly-OCH3 is described

()RG·ANIC CHEMISTRY IN PEPTIDE SYNTHESIS J. RuniNGER Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy oj Science, Prague, Czechoslovakia INTRODUCTION There is a widely held impression among organic chemists that peptide synthesis is a craft or mystery with a symbolism, language, and ritual all it:; own, something quite remote from the interests of those working in other fields. On occasions such as this Congress, which bring tagether chemists ir:,terested in a great diversity of special subjects, it should be our aim to cl

Solid Phase Peptide Synthesis by Four Component Condensation: Peptide Formation on an Isocyano Polymer Support Reza Arshady* and Ivar Ugi Organisch-chemisches Institut der Technischen Universität München, Lichtenbergstraße 4, D-8046 Garching, W.-Germany Z. Naturforsch. 36b, 1202-1203 (1981); received May 4, 1981 Solid Phase Peptide Synthesis, Four Component Condensation, Isocyano Polymer Support, Anchoring Technique Coupling of various protected amino acids or small peptides on an isocyano polymer and in the presence of 1 -methyl-3-formylindole

Pure & Appl. Chem., Vol. 68, No. 6, pp. 1335-1339, 1996. Printed in Great Britain. Q 1996 IUPAC Proteinases as catalysts in peptide synthesis V.M.S tepanov Institute of Genetics and Selection of Industrial Microorganisms, I 13545, Moscow, Chemistry Department of Moscow State University, Moscow, Russia ABSTKACT Proteolytic enzymes application as efficient catalysts of peptide synthesis is discussed. Serine proteinases - subtilisin and chymotrypsin turned to be especially efficient for kinetically controlled synthesis by condensation of peptide estcrs and

NUCLEOPHILE BINDING IN CHYMOTRVPSIN PEPTIDE SYNTHESIS D.D. Petkov, E.K. Bratovanova and I.B. Stoineva Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, 1040 Sofia, BULGARIA Introduction The asymmetric peptide synthesis, catalysed by proteinases, is de- termined by the specific binding of the amine component (nucleophi- le) to the enzyme 1eaving-group binding site. We report here an ob- servation of a kinetic saturation of the enzyme by the nucleophile. Such saturation kinetics is consistent both with a mechanism

ADAPTATION OF SIDE REACTIONS FOR PEPTIDE SYNTHESIS Miklos Bodanszky, Maria A. Bednarek,Ai-xue Ji, Agnes Bodanszky Department of Chemistry, Case Western Reserve University Cleveland, Ohio, 44106, U.S.A. We attempted to put to good use some side reactions observed in peptide synthesis by adapting them for processes of protec- tion and deprotection. Protection The often reported alkylation of the methionine side chain was exploited for reversible blocking of the thioether function. In order to have no doubt about the S-alkyl group which re- mains after

NEW SUPPORTS FOR SOLID-PHASE PEPTIDE SYNTHESIS R.P. Evstigneeva, E.I. Filippovich, E.N. Zvonkova Lomonosov Institute of Fine Chemical Technology, Moscow, USSR Introduction Modern peptide chemistry possesses two principal methods of higher peptide synthesis: these are the classical method and the solid- phase technique. It is not an easy matter to give preference to either of the methods, as both have their merits and demerits. Yet it should be ncL.;d that the majority of successful syntheses of biologically active peptides had been achieved by solid

APPLICATION OF PHOSPHINIC ACIDS TO PEPTIDE SYNTHESIS R. Ramage, C. Ashton, B. Atrash, D.Hopton and M.J.Parrott Department of Chemistry, UMIST, PO Box 88, Manchester M60 1QD The central problems of peptide synthesis are the choice of temporary protection for side-chain functionality, with the requirement of complementarity to the Na protecting groups, and the method selected for activation of carboxylic acid functions towards amide formation. Organophosphorus and organosilicon chemistry have great potential in both these aspects of methodology since P and