Abstract: Analogs of CRF, which are based upon hCRF, oCRF, sauvagine and alpha-helical CRF, are disclosed that can be administered to achieve a substantial elevation of ACTH, .beta.-endorphin, .beta.-lipotropin, other products of the pro-opiomelanocortin gene and corticosterone levels and/or an increase in blood pressure over an extended period of time. One CRF agonist which has been found to be particularly potent is: H-Ser-Gln-Glu-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-D-Phe-His-Leu-Leu-Arg-Glu-Va l-Leu-Glu-Met-Thr-Lys-Ala-Asp-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-L eu-Leu-Asp-Ile-Ala-NH.sub.2. In these agonist analogs, one or more of the first six N-terminal residues may be deleted and/or the N-terminal alpha-amino group may be acylated by an acylating agent containing up to 7 carbon atoms. A number of other substitutions may also be made throughout the chain.

Abstract: A biologically active peptide which includes the following structure:R.sub.1 --R.sub.1 --R.sub.1 --R.sub.3 --R.sub.5 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 R.sub.3 --R.sub.1 --R.sub.4 --R.sub.1 --R.sub.3 --R.sub.4 --R.sub.1 --R.sub.1.R.sub.1 is a hydrophobic amino acid, R.sub.2 is a basic hydrophilic amino acid, and R.sub.3 is a neutral hydrophilic amino acid, R.sub.4 is a hydrophobic or basic hydrophilic amino acid, and R.sub.5 is a hydrophobic, basic hydrophilic, or neutral hydrophilic amino acid.Examples of such peptides include the following:(SEQ ID NO:1)--NH.sub.2 ;(SEQ ID NO:2)--NH.sub.2 ;(SEQ ID NO:3)--NH.sub.2 ;(SEQ ID NO:4)--NH.sub.2 ;(SEQ ID NO:5)--NH.sub.2 ;(SEQ ID NO:6)--NH.sub.2 ;(SEQ ID NO:7)--NH.sub.2 ; and(SEQ ID NO:8).The peptides may be employed in pharmaceutical compositions.

Abstract: This invention provides novel growth hormone-releasing peptides and a method for increasing the release and raising the levels of growth hormone in mammals. The invention also provides a method for increasing the growth rate of meat producing animals, treating the symptoms of growth hormone deficiencies in mammals and improving the efficiency of feed utilization by meat producing and dairy animals.

Abstract: Several known members of the corticotropin releasing factor (CRF) family have been synthesized and tested, including human and rat CRF which have the formula: H-Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-Phe-His- Leu-Leu-Arg-Glu-Val-Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln- Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-Glu- Ile-Ile-NH.sub.2. Peptides are herein disclosed that are potent competitive antagonists of CRF in mammals. One which has been found to be particularly potent is: H-D-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Nle-Ala- Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn- Arg-Lys-Leu-Nle-Glu-Ile-Ile-NH.sub.2. One that has shown particularly prolonged duration of potency is: H-D-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Nle-Ala- Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn- Arg-Lys-CML-Nle-Glu-Ile-Ile-NH.sub.2.

Abstract: The present invention relates to the use of peptide hormone analogues as inhibitors of their respective naturally occurring peptide hormone. The structure of the peptide hormone analogues is exemplified by parathyroid hormone (PTH), wherein Lys.sup.13 is substituted to increase the biological activity of the PTH analogues. Thus, there are disclosed peptides having the formulae:PTH(7-34)NH.sub.2 ;[Tyr.sup.34 ]PTH(7-34)NH.sub.2 ;[D-Trp.sup.12, Tyr.sup.34 ]PTH(7-34)NH.sub.2 ;[Nle.sup.8,18, D-Trp.sup.12, Tyr.sup.34 ]PTH(7-34)NH.sub.2 ;[Nle.sup.8,18, Tyr.sup.34 ]PTH(7-34)NH.sub.2 ;desamino[Nle.sup.8,18, D-Trp.sup.12, Tyr.sup.34 ]PTH(7-34)NH.sub.2 ; and,desamino[Nle.sup.8,18, D-Trp.sup.12, Tyr.sup.34 ]PTH(8-34)NH.sub.2wherein Lys.sup.13 is modified in the epsilon-amino acid group by N,N-diisobutyl or 3-phenylpropanoyl.