Abstract: A peptide effective in blocking the CXC-chemokine receptor 4 (CXCR4) mediated HIV-1 NL4-3 (X4-tropic) infection with an IC50 value of less than 50 ?M.

Abstract: An N-terminally protected peptide having the sequence (SEQ ID NO: 1) X-Glu-Cys-Lys-Ile-Lys-Gln-Ile-Ile-Asn-Met-Trp-Gln, wherein X is a group protecting the N-terminal of the peptide.

Abstract: An N-terminally protected peptide having the sequence (SEQ ID NO: 1) X-Glu-Cys-Lys-Ile-Lys-Gln-Ile-Ile-Asn-Met-Trp-Gln, wherein X is a group protecting the N-terminal of the peptide.

Abstract: A process for preparing human relaxin-2 having the following amino acid sequence: A chain: (SEQ?ID?NO:?1) pGlu-Leu-Tyr-Ser-Ala-Leu-Ala-Asn-Lys-Cys-Cys-His- Val-Gly-Cys-Thr-Lys-Arg-Ser-Leu-Ala-Arg-Phe-Cys B chain: (SEQ?ID?NO:?2) Asp-Ser-Trp-Met-Glu-Glu-Val-Ile-Lys-Leu-Cys-Gly- Arg-Glu-Leu-Val-Arg-Ala-Gln-Ile-Ala-Ile-Cys-Gly- Met-Ser-Thr-Trp-Ser; comprising the following steps: providing the amino acids necessary for the synthesis of the A and B chains with usual protective groups, wherein the cysteines are employed as trityl-protected amino acids (L-Cys(Trt)-OH); effecting a chromatographic purification of the individual chains A and B after the solid state synthesis; followed by the simultaneous folding and combination of the individual chains A and B in ammonium hydrogencarbonate buffer at pH 7.9 to 8.4; and subsequent purification of the relaxin-2 formed.

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: A serine protease inhibitor, characterized by having a domain with four cysteines, and a sequence of 0 to 20 amino acids is present between the first and second cysteines, or the serine protease inhibitor has a domain with six cysteines, and a sequence of 7 to 20 amino acids is present between the first and second cysteines.

Abstract: The present invention relates to antibiotically active natriuretic peptides for use as antibiotically active preparations prepared using biotechnological and recombinant methods and chemical synthesis. The antibiotically active peptides are referred to as natriubiotics. After chemical peptide synthesis, these natriubiotics can be used as human or veterinary medicaments in a suitable galenic formulation or as food additives.

Abstract: The invention relates to serine protease inhibitors having the amino acid sequence in accordance with Seq. ID No. 1.

Abstract: Pepetides having bifidogenic properties are obtainable by the process of adding proteases to cow'milk or human milk, followed by incubation, centrifugation, acidification, purification by reverse phase HPLC and cation-exchange HPLC, culturing Bifidobacterium bifidum and E. coli in the presence of collected bifidogenic fractions, and isolation of the peptides having bifidogenic properties, and the isolated peptides can be amidated, acetylated, sulfated, phosphorylated, glycosylated, oxidized, or fragmented and still maintain their bifidogenic properties, and combination peptides having bifidogenic properties are obtainable by chemically bonding the peptides having bifidogenic properties, the amidated, acetylated, sulfated, phosphorylated, glycosylated, oxidized, or fragmented peptides having bifidogenic properties, or combinations thereof.

Abstract: Use of urodilatin for treating chronic renal insufficiency by stimulating the residual renal function.

Abstract: The present invention relates to a quick method for the qualitative and quantitative medical-diagnostic analysis on the protein level of the substitution of single amino acids with pathogenic and non-pathogenic effects on the organism. The medical-diagnostic analysis is performed by a combination of enzymatic or chemical cleavage of the isolated peptide, chromatographical separation of the fragments and analysis by mass spectrometry, both direct LC/MS and indirect MALDI-MS, and analysis by capillary electrophoresis. By comparing protein samples from healthy humans with those of ill humans, the method described is suitable for establishing new, as yet unknown mutations and quantifying the expression and incorporation of wild type to mutant.