Abstract: A process for preparing polyaspartic acid by polycondensation of fine-particle aspartic acid at temperatures above 150.degree. C. in the presence of acidic catalysts, wherein first contact between the acidic catalysts and the fine-particle aspartic acid takes place in the reaction zone where the polycondensation takes place.

Abstract: This invention provides processes for the synthesis of platelet glycoprotein IIb/IIIa inhibitors and intermediate compounds useful in said processes.

Abstract: Compositions and methods of incorporating ligand precursors and ligands at any location within a peptide during peptide synthesis are disclosed. Derivatives of 2,4,5-triaminopentanoic acid and .gamma.-aminoglutamic acid are selectively incorporated into the peptide during solid phase or liquid phase synthesis, depending upon the choice of protecting groups. Ligand synthesis may then be completed at a later time to produce N.sub.3 S, N.sub.2 S.sub.2, and EDTA type chelating agents.

Abstract: The present invention is drawn to a process for forming an amide bond linkage comprising reacting a carboxylic acid and an amine in a two-phase mixture of water and an organic solvent selected from an oxygenated organic solvent or an aromatic solvent in the presence of a coupling reagent and an additive. This process is useful for making ubiquitous amides and polypeptides having various biological activities.

Abstract: The invention relates to a process for the preparation of cardiodilatin fragments, to highly purified cardiodilatin fragments, and to appropriate intermediates for the preparation of said fragments. Furthermore, the invention relates to highly purified cardiodilatin fragments which are free of peptide impurities and exhibit a single migration peak in capillary electrophoresis, as well as to appropriate processes for the preparation of same.

Abstract: This invention relates to a method of inverse solid phase synthesis in which reactants are reacted in solution and a solid phase matrix is used to separate unreacted reactants from desired product.

Abstract: A method is provided for preparing decapeptide and undecapeptide derivatives of LHRH by solution phase peptide chemistry as well as intermediate peptides useful in the same method.

Abstract: A method is provided for preparing decapeptide and undecapeptide derivatives of LHRH by solution phase peptide chemistry as well as intermediate peptides useful in the same method.

Abstract: This invention relates to a process for forming an amide or an ester from a reaction between an amine or an alcohol, respectively and an acylating derivative of a carboxylic acid, in the presence of an effective amount of a compound having the formula: ##STR1## and N-oxides thereof and salts thereof.

Abstract: Described is a peptide fragment which comprises the amino acid sequence 95-126 of ANF/CDD 1-126 (gamma-hANaP) and is formed in the kidney. The fragment urodilatin (ANF/CDD 95-126) has the following amino acid sequence: ##STR1## wherein R.sup.1 and R.sup.2 each represent further peptide fragments of ANF/CDD 1-126 (gamma-hANaP). In the amino acid sequence R.sup.1 is Thr-Ala-Pro-Arg-Ser-Leu-Arg-Arg-Ser-Ser and R.sup.2 is Asn-Ser-Phe-Arg-Tyr. Further described are processes for the preparation and/or recovery of the new peptide fragment and a medicament containing urodilatin (ANF/CDD 95-126) as well as medical indications of the medicament.

Abstract: This invention relates to a process for forming an amide or an ester from a reaction between an amine or an alcohol, respectively and an acylating derivative of a carboxylic acid, in the presence of an effective amount of a compound having the formula: ##STR1## and N-oxides thereof and salts thereof.

Abstract: A solid phase coupling reagent for amide formation, comprising insoluble polymer bearing pendant side chains, said side chains each comprising a terminal portion having the formula ##STR1## wherein Y.sup.- is a counteranion and n is independently an integer from 2 to 6; and a method of making amides employing the coupling reagent.

Abstract: A method of chemical ligation of peptides that requires no side chain protecting groups and no activation of the C-.alpha. carboxyl group is presented. The method consists of three steps. In the first step, initiation, a masked glycoaldehyde ester is enzymatically or chemically coupled to the C-terminal carboxylic acid of an sidechain unprotected first peptide. In the second step, ring formation, the masked aldehyde ester of the first peptide is unmasked, and then reacted with the N-.alpha. amino acid of a second sidechain unprotected peptide to form a ring structure. In the third step, rearrangement, the O-acyl ester linkage transfers at higher pH to an N-acyl linkage on the ring to form a peptide bond.

Abstract: Process for the diastereoselective reductive pinacol coupling of homochiral .alpha.-aminoaldehydesA process for the preparation of optically pure symmetrical compounds of the formula I ##STR1## is described, in which R.sup.1, R.sup.2 and R.sup.3, are explained in the description, with simultaneous control of the four centers of chirality indicated by *.

Abstract: The method of the invention provides for the formation of a recombinant polypeptide which has been modified at the C-terminal end through the use of a transpeptidation process. The method is suitable for modifying recombinant polypeptides of any source including those which may be commercially available, those derived from recombinant single copy or multicopy polypeptide constructs, or those derived from single or multicopy recombinant fusion protein constructs. The transpeptidation reaction involves contacting an endopeptidase enzyme with a recombinant polypeptide to substitute an addition unit, of one or more amino acids, for a leaving unit, linked to a core polypeptide through a cleavage site recognized by the endopeptidase enzyme. Recombinant polypeptides derived from multicopy polypeptide constructs may be cleaved from the multicopy polypeptide at the N-terminal and C-terminal ends and simultaneously under go substitution of the leaving unit by the desired addition unit.

Abstract: A peptide of the following general formula is subjected to cyclization reaction to produce a cyclic peptide, preferably a synthetic calcitonin derivative (elcatonin) which is a useful medicine. ##STR1## (wherein A and B form a peptide of the formula Ser-Asn-Leu-Ser-Thr (SEQ ID NO: 43); X means a hydroxyl group, a carboxy-protecting group, an amino acid residue or a peptide residue; provided that the side-chain carboxyl group of .alpha.-L-aminosuberic acid is condensed with an amino acid or a peptide). The cyclic peptide can be obtained by subjecting a peptide of the above general formula to (1) cyclization reaction by chemical condensation, (2) cyclization reaction in the presence of an alkali metal salt and (3) reactions using the techniques of liquid phase synthesis and solid phase synthesis in combination.

Abstract: The present invention is drawn to a process for forming an amide bond linkage comprising reacting a carboxylic acid and an amine in a two-phase mixture of water and an organic solvent selected from an oxygenated organic solvent or an aromatic solvent in the presence of a coupling reagent and an additive. This process is useful for making ubiquitous amides and polypeptides having various biological activities.

Abstract: A method for synthesizing polypeptides from amino acids and/or peptides utilizing a novel reaction medium containing a hydrated silica entity containing silanol groups which function as an inorganic enzyme.

Abstract: In this invention, a peptide of the following general formula is subjected to cyclization reaction to produce a cyclic peptide, preferably a synthetic calcitonin derivative (elcatonin) which is a useful medicine. ##STR1## (wherein A and B form a peptide of the formula Ser-Asn-Leu-Ser-Thr (SEQ ID NO: 47); X means a hydroxyl group, a carboxy-protecting group, an amino acid residue or a peptide residue; provided that the side-chain carboxyl group of .alpha.-L-aminosuberic acid is condensed with an amino acid or a peptide).The cyclic peptide can be obtained by subjecting a peptide of the above general formula to (1) cyclization reaction by chemical condensation, (2) cyclization reaction in the presence of an alkali metal salt and (3) reactions using the techniques of liquid phase synthesis and solid phase synthesis in combination.

Abstract: A solid phase coupling reagent for amide formation, comprising insoluble polymer bearing pendant side chains, said side chains each comprising a terminal portion having the formula ##STR1## wherein Y.sup.- is a counteranion and n is independently an integer from 2 to 6; and a method of making amides employing the coupling reagent.

Abstract: A solution phase process for making peptides having biological activity or peptide intermediates which can be used to prepare peptides having biological activity is described. The process involves the condensation reaction of two peptide fragments.

Abstract: Polyaspartic acid having a weight average molecular weight of 1000 to 5000 is produced by hydrolysis of anhydropolyaspartic acid. Anhydropolyaspartic acid is produced by condensation polymerization of L-aspartic acid. Greater than 80% conversion is achievable utilizing "temperature vs time" profiles.

Abstract: New retro-inverso analogs of thymopentin (TP5) and of its tripeptide fragment (TP5.sup.1-3) of general formula (I) ##STR1## are described wherein R is hydrogen or an acyl radical, and R.sup.1 is --OR.sup.2 or ##STR2## wherein R.sup.2 is hydrogen or a hydrocarbyl radical, and the corresponding pharmaceutically acceptable acid- or base-addition salts. A process of preparing the tripeptide fragment of formula I is also described.The new compounds are enzyme-resistant immunomodulatory peptides.

Abstract: A process is provided for purifying Urogenital Sinus Derived Growth Inhibitory Factor (UGIF) from embryonic tissue which comprises chromatographing medium from cultures of embryonic tissue derived from the urogenital sinus by gel filtration chromotography. Further purification by reverse phase high pressure liquid chromotography is also demonstrated. The UGIF is obtained in 70-fold to 8000-fold purification over the conditioned medium. A UGIF composition of matter is also provided.

Abstract: Peptide preparation is carried out by a continuous process by supplying a serine protease or peptidase enzyme retained in a reaction vessel with an alkyl ester of an N-protected amino acid or oligopeptide and a recycle stream containing an amino acid or oligopeptide to form an N-protected chain extended peptide, separating the N-protected chain extended peptide by adsorption on a hydrophobic absorbent, and eluting and recovering the adsorbed N-protected chain extended peptide. Adsorption is carried out without adjusting the pH from that in the reaction vessel, and adsorber effluent is recycled to the recycle stream. The protease or peptidase enzyme may be immobilized, and there is substantial exclusion of organic solubilizers in the reaction vessel. A preferred N-protecting group is an N-phenacyl group. The N-protecting group can be separated from the N-protected chain extended peptide with a deprotecting enzyme to recover the chain extended peptide.

Abstract: The invention relates to a process for the preparation of protected arginine-containing peptides by fragment coupling, at least one arginine-containing fragment being reacted as perchlorate, and to protected secretin derivatives of the formula I described.

Abstract: The invention relates to a process for the preparation of peptides of the formula IU--A.sup.1 --A.sup.2 13 A.sup.3 --A.sup.4 --A.sup.5 --X (I)in whichU denotes a urethane protective group,A.sup.1 denotes Trp or D-Trp,A.sup.2 denotes Ser, Ala or Thr,A.sup.3 denotes Tyr or Phe,A.sup.4 denotes Gly, the residue of a D-amino acid or the residue of a D-amino acid derivative,A.sup.5 denotes Leu, N-methyl-Leu, N-ethyl-Leu, Ser(Bu.sup.t), Cys(But), Asp(OBu.sup.t), Glu(OBu.sup.t), Orn(Boc) or Lys(Boc) andX denotes OBu.sup.t or A.sup.6 --Pro--Y,whereA.sup.6 represents Arg, Orn, Lys or homoarginine, andY represents Gly--NH.sub.2, NH--NH--CO--NH.sub.2, (C.sub.1 -C.sub.3)-alkylamino, cyclopropylamino, (C.sub.1 -C.sub.3)-alkylamino which is substituted with hydroxyl or fluorine, or cycloalkylamino which is substituted with hydroxyl or fluorine, using tripeptides of the formula II,U--A.sup.1 --A.sup.2 --A.sup.3 --OH,in which the residues are defined as above.

Abstract: An active protein can be easily, safely produced by a method comprising providing a first peptide fragment having a first amino acid sequence corresponding to part of an active protein and a second peptide fragment having a second amino acid sequence corresponding to the remaining part of the active protein, at least one of said first peptide fragment and said second peptide fragment being one which has been obtained by recombinant DNA technique or has been obtained by a method comprising producing a predetermined peptide fragment by recombinant DNA technique and deleting from or adding to said predetermined peptide fragment at its N-terminus at least one amino acid residue; and linking said first peptide fragment at its C-terminus to said second peptide fragment at its N-terminus.

Abstract: The invention relates to a process for the preparation of peptides of the general formulaArg--Lys--S--Val--Yin which S denotes glutamic acid or .alpha.-aminoadipic acid and Y denotes tyrosine or tryptophan or esters or amides thereof, which comprises subjecting tetrapeptides of the formulaZ--Arg(Z'.sub.2)--Lys(Z')--S--(Bzl)--Val--OHin which Z' represents a protective group of the benzyl type, to a condensation reaction with corresponding tyrosine esters or amides or tryptophan esters or amides and removing the protective groups by hydrogenation. The invention furthermore relates to tetrapeptides as intermediate products of this process.