Abstract: A method for the separation of at least one specific binding entity from a mixture of binding entities, which comprises the steps of contacting said mixture of binding entities with an immobilized peptide in which said peptide specifically binds to said specific binding entity, and separating the immoblized peptide/specific binding entity complex from the mixture of binding entities; an immobilized peptide-solid support preparation comprising a cleavable link between the peptide and the solid support, and a method for the preparation of a peptide from an immobilized peptide-solid support preparation.

Abstract: The present invention is directed to the use of a cyclopropylmethyl derivative as a protecting group for compounds containing an amino group, carboxy group, amido group, mercapto group or hydroxy group and to the compounds formed having the cyclopropylmethyl moiety as the protecting group.

Abstract: A procedure for the preparation of salmon calcitonin comprising the condensation of fragment 1(SEQ ID NO: 1), a docosapeptide corresponding to the carboxamide end of the salmon calcitonin sequence conveniently protected and anchored on resin, with fragment 2(SEQ ID NO:2), a decapeptide corresponding to the amino end of the salmon calcitonin sequence conveniently protected and with a disulphide bridge ready formed between the two cysteines, and the treatment of the complete peptide skeleton (fragment 6 (SEQ ID NO:6)) with an acid to liberate the totally deprotected peptide from the resin.

Abstract: The present invention provides a group of novel compounds that inhibit the proteolytic activity of 3C proteases which are found in picornaviruses, particularly rhinoviruses. In picornaviruses the RNA genome is translated into a single large viral polyprotein precursor. The precursor demonstrates auto-proteolytic activity, cleaving itself into mature viral gene products. Therefore, compounds of the current invention are particularly useful in treating picornaviral infections by interrupting the processing of the viral gene products into mature and infectious viral particles. The current invention also provides a novel process the preparation of compounds of the current invention. The process entails the selective reduction of an imide intermediate representing a marked improvement over processes known in the art for making peptidyl-aldehydes.

Abstract: Compounds of formula I are described, ##STR1## wherein n is equal to one or two, R.sub.1 stands for hydrogen or an amino protecting group, R.sub.2 represents hydrogen or a carboxyl protecting group and R.sub.3 4-methyltriphenylmethyl, 4,4'-dimethyltriphenylmethyl, 4,4',4"-trimethyltriphenylmethyl. Furthermore described are compounds of formula I which are reactive and suitable for coupling reactions and are derived from I with R.sub.2 =H by activation of the carboxyl group.The compounds mentioned above can be used as starting materials for the synthesis of peptides. They are more suitable than analogous compounds of formula I, wherein R.sub.3 represents hydrogen or a carbamoyl protecting group used hitherto.

Abstract: A new amino acid derivative, N.sup..alpha. -tert-butoxycarbonyl-N.sup.e -(N-bromoacetyl-.beta.-alanyl)-L-lysine (BBAL), has been synthesized as a reagent to be used in solid-phase peptide synthesis for introducing a side-chain bromoacetyl group at any desired position in a peptide sequence. The bromoacetyl group subsequently serves as a sulfhydryl-selective cross-linking function for the preparation of cyclic peptides, peptide conjugates and polymers. BBAL residues are stable to final HF deprotection/cleavage. BBAL peptides can be directly coupled to other molecules or surfaces which possess free sulfhydryl groups by forming stable thioether linkages. Peptides containing both BBAL and cysteine residues can be self-coupled to produce either cyclic molecules or linear peptide polymers. Such peptide derivatives are useful in preparing potential peptide immunogens, vaccines and therapeutics, and for substances such as peptides linked to polymers, plastics, enamels and ceramics.

Abstract: Peptides immunoreactive with antibodies to native proteins, and which have at least two cysteine residues that contribute to mimicking an epitope of the protein, are prepared with the cysteine thiol groups protected. When deprotected, the peptides have enhanced immunoreactivity. The peptides are particularly useful for detecting antibodies or antigens associated with retroviruses, including the clinically important lymphotropic retroviruses HIV-1, HIV-2, HTLV-I, and HTLV-II.

Abstract: The present invention provides a process for the preparation of peptides which have or side-chains containing an alkyl- or dialkyl-substituted guanidinyl group or a imidazinylamino or tetrahydropyrimidinylamino group. The process provides higher overall yields of peptide product by permitting the synthesis of the entire peptide chain prior to modification of the side-chain to introduce the groups.

Abstract: The present invention relates to novel peptides of formulaeXaa Glu Asp Cys Lys (SEQ I.D. No: 1),andGlu Asp Cys Lys (SEQ I.D. No: 2)wherein the Cys sulfur is bonded to an acetamidomethyl group, and Xaa is pyro-Glu, the acid addition salts thereof, the pharmaceutical compositions comprising the same and a process for the preparation of the novel peptides and compositions.The novel peptides selectively inhibit the proliferation of hemopoietic cells.The invention also covers the treatment of mammals (including human beings) with the said peptides and compositions for selectively inhibiting the proliferation of hemopoietic cells.The advantage of the novel compounds is that they are almost completely harmless, they do not have any side-effect in therapeutic dose-range, in addition they significantly inhibit the damaging effects of drugs and radiation used for the therapy of tumorous diseases or the dose of drug or radiation can be increased when they are administered.

Abstract: A new amino derivative, N.sup..alpha. -tert-butoxycarbonyl-N.sup..epsilon. -(N-bromoacetyl-.beta.-alanyl)-L-lysine (BBAL), has been synthesized as a reagent to be used in solid-phase peptide synthesis for introducing a side-chain bromoacetyl group at any desired position in a peptide sequence. The bromoacetyl group subsequently serves as a sulfhydryl-selective cross-linking function for the preparation of cyclic peptides, peptide conjugates and polymers. BBAL residues are stable to final HF deprotection/cleavage. BBAL peptides can be directly coupled to other molecules or surfaces which possess free sulfhydryl groups by forming stable thioether linkages. Peptides containing both BBAL and cysteine residues can be self-coupled to produce either cyclic molecules or linear peptide polymers. Such peptide derivatives are useful in preparing potential peptide immunogens, vaccines and therapeutics, and for substances such as peptides linked to polymers, plastics, enamels and ceramics.

Abstract: Oligomers and polymers are prepared substantially free of error sequences by sequentially adding monomers, which are terminally blocked and have active functionalities protected, to a growing chain bound to a support through a selectively cleavable linkage. After each addition, unblocked terminal groups are capped. At the completion of monomer addition, enzymatic hydrolysis interfering protecting groups are removed along with the capping group and failure sequences enzymatically degraded. The terminal blocking group may then be removed. The completed oligomer or polymer may be cleaved from the support prior or subsequent to enzymatic degradation but after completion of the sequence.

Abstract: A method for cyclization and reversal of the polarity of polymers on a substrate. The method provides for the formation of a polymer on a substrate (2) with a tether molecule (4). Through unmasking of a protective group (PG.sub.2) a cyclic polymer (6) is formed. Through cleavage of an appropriate bond, a polarity reversed polymer (8) is formed. The method finds particular application in the formation of, for example, peptides and oligonucleotides.

Abstract: A process for producing an amide or an ester represented by the general formula W-A-B-Y which involves reacting an ester sulfonium salt represented by the general formula: ##STR1## with a nucleophilic agent represented by the general formulaH--B--Ywherein B represents a nucleophilic group, and wherein the members of the formula are further described in detail in the specification.

Abstract: Gla.sup.17 human osteocalcin and Glu.sup.17 human osteocalcin or salts thereof are prepared by introducing .gamma.-carboxyglutamic acid into the amino acid sequence of said osteocalcin by employing a protective L-.gamma.-carboxyglutamic acid represented by the formula: ##STR1## wherein n represents 0, 1 or 2, or a salt thereof in the appropriate position in the reacting sequence of amino acids which form the osteocalcin.

Abstract: Polypeptide arrays can be synthesized on a substrate by attaching photoremovable groups to the surface of a substrate, exposing selected regions of the substrate to light to activate those regions, attaching an amino acid monomer with a photoremovable group to the activated regions, and repeating the steps of activation and attachment until polypeptides of the desired length and sequences are synthesized. The resulting array can be used to determine which peptides on the array can bind to a receptor.

Abstract: The present invention provides a stable and bioactive somatotropin which has its small-loop sulfhydryl groups derivatized and a method for producing the small-loop derivatized somatotropin. The small-loop derivatized somatotoropin is stable during long term storage, i.e. it forms very few dimers, oligomers, and aggregates which inactivate the somatotropin, and has a bioactivity equal to or greater than that of the non-derivatized somatotropin.

Abstract: A method to incorporate bromoacetyl and chloroacetyl moieties on amino groups of synthetic peptides using a standard program with an automated peptide synthesizer has been developed. The bromoacetyl and chloroacetyl-derivatized peptides react well with sulfhydryl-containing proteins and with peptides containing cysteine residues. Autopolymerization or cyclization occurs by reaction of the free sulfhydryl of cysteine in a peptide with the bromoacetyl group (or chloroacetyl group) and reactions can generally be controlled by controlling the concentrations of starting peptide in neutral pH buffers. Analytical methods for evaluating the polymers or cyclized peptides include gel filtration chromatography, reverse phase HPLC, SDS-PAGE and amino acid analysis where the degree of reaction can be evaluated by quantifying the amount of S-carboxymethylcysteine formed after HCl hydrolysis.

Abstract: A method of promoting and accelerating the healing of bones in animals utilizing an effective amount of a GHL-(Cu) pharmicuetical composition is disclosed. Also methods of inducing the formulation of granulation tissue in affected bones of animals using a GHL-(Cu) composition is disclosed.

Abstract: The invention provides a method and reagent for the modification of polypeptides useful in experimental research in the area of genetic engineering starting from a polypeptide such as hCCK-33 in an unsulfated form which contains Tyr and Ser and/or Thr residues by first protecting the amino-groups in the starting polypeptide, masking the OH-groups in the Ser and/or Thr residues and selectively sulfating the OH-groups in the Tyr residues after deprotection.

Abstract: A method for the solid phase synthesis of multi-sulfated peptides comprising coupling side-chain unprotected hydroxyamino acids to the peptide chain utilizing benzotriazol-1-yl-oxy-tris (dimethyl)-phosphonium hexafluorophosphate (BOP) as a coupling reagent.

Abstract: Process for preparing antibiotic L, 17392 by catalytically hydrogenating a deglucoteicoplanin ester of formula ##STR1## wherein A, B and Z represent hydrogen atoms, R represents benzyl or substituted benzyl, wherein the phenyl group is substituted with at least a substituent selected from chloro, bromo, fluoro, nitro, (C.sub.1 -C.sub.3)alkyl, (C.sub.1 -C.sub.3)alkoxy and the like, with the exclusion of the tri-nitro phenyl group, or acid addition salts thereof, to catalytic hydrogenolysis in the presence of a poisoned hydrogenation catalyst at a temperature from 10.degree. C. to 40.degree. C. and a pressure between ambient pressure and 5 atm, in an inert organic solvent preferably in the presence of a mineral acid.

Abstract: A method for the synthesis of sulfydryl-containing peptides which comprises forming a benzylthioether-linked solid support-bound thiol compound having at least one functional group for generating at least one peptide bond, sequentially coupling at least one protected amino acid or peptide to the compound until a peptide having desired amino acid sequence is obtained, and cleaving the benzylthioether linkage to release the peptide from the support with concomitant regenertion of the sulfydryl group in the peptides. The invention also encompasses compounds having the general formula ##STR1## wherein X is H, NH.sub.2, ##STR2## or acyl-NHY, said acyl being an amino acid or a peptide; Y is H, COOH, CONHNH.sub.2, ##STR3## the ester COOR.sup.1 in which R.sup.1 is selected from the group consisting of methyl, ethyl, phenyl, ortho-nitrophenyl and para-nitrophenyl, the amide CONH.sub.2, or the amide CONHR.sup.2 in which R.sup.2 is an amino acid or peptide; and providing that X and Y cannot both be H.

Abstract: A method is provided for quantitatively monitoring the deprotection and coupling reactions employed in the solid phase synthesis of peptides. The method entails synthesizing a peptide on a support matrix that has a first marker associated therewith. The amino acids employed in the peptide synthesis procedure have a second marker attached thereto, which can be the blocking group used for the amino acid. After the coupling or deprotection step a portion of the support matrix is processed to release first and second identifers from the first and second markers, respectively. The completeness of the coupling or deprotection step can be determined by comparing the relative amounts of the detected first and second identifiers. Novel compositions of matter are used in or produced during this method, including support matrixes having pyrolyzable markers attached thereto.

Abstract: The invention concerns new 1-tert.-alkyl-thiohydrazine-1,2-dicarboxylic a derivatives, their production, and their use as reagents for the transfer of a 1-tert.-alkylthio residue, particularly of a 1-tert.-butylthio residue as a protective group for thiols.