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Application Area

GRF (1-29) amide (rat)

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

Others

Catalog number

BAT-015922

CAS number

91826-20-9

Molecular Formula

C155H251N49O40S

Molecular Weight

3473.02

Specification
Reference Reading

IUPAC Name

(4S)-4-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-imidazol-4-yl)propanoyl]amino]propanoyl]amino]-3-carboxypropanoyl]amino]propanoyl]amino]-3-methylpentanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylpentanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]-5-carbamimidamidopentanoyl]amino]hexanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-5-[[(2S,3S)-1-[[(2S)-1-[[(2S)-4-amino-1-[[(2S)-1-amino-5-carbamimidamido-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-5-oxopentanoic acid

Synonyms

H-His-Ala-Asp-Ala-Ile-Phe-Thr-Ser-Ser-Tyr-Arg-Arg-Ile-Leu-Gly-Gln-Leu-Tyr-Ala-Arg-Lys-Leu-Leu-His-Glu-Ile-Met-Asn-Arg-NH2

Appearance

White Powder

Purity

95%

Sequence

HADAIFTSSYRRILGQLYARKLLHEIMNR

Storage

-20ºC

InChI

InChI=1S/C155H251N49O40S/c1-20-80(12)120(201-127(220)85(17)180-138(231)112(68-119(215)216)189-126(219)83(15)178-128(221)94(157)65-90-69-169-74-176-90)149(242)198-109(62-87-32-24-23-25-33-87)145(238)204-123(86(18)207)151(244)200-114(73-206)147(240)199-113(72-205)146(239)194-108(64-89-41-45-93(209)46-42-89)142(235)186-98(37-30-55-173-154(165)166)131(224)185-99(38-31-56-174-155(167)168)135(228)202-122(82(14)22-3)150(243)197-103(58-76(4)5)129(222)175-71-117(212)181-100(47-49-115(158)210)133(226)191-105(60-78(8)9)140(233)193-107(63-88-39-43-92(208)44-40-88)137(230)179-84(16)125(218)183-97(36-29-54-172-153(163)164)130(223)184-96(34-26-27-52-156)132(225)190-104(59-77(6)7)139(232)192-106(61-79(10)11)141(234)195-110(66-91-70-170-75-177-91)143(236)187-101(48-50-118(213)214)136(229)203-121(81(13)21-2)148(241)188-102(51-57-245-19)134(227)196-111(67-116(159)211)144(237)182-95(124(160)217)35-28-53-171-152(161)162/h23-25,32-33,39-46,69-70,74-86,94-114,120-123,205-209H,20-22,26-31,34-38,47-68,71-73,156-157H2,1-19H3,(H2,158,210)(H2,159,211)(H2,160,217)(H,169,176)(H,170,177)(H,175,222)(H,178,221)(H,179,230)(H,180,231)(H,181,212)(H,182,237)(H,183,218)(H,184,223)(H,185,224)(H,186,235)(H,187,236)(H,188,241)(H,189,219)(H,190,225)(H,191,226)(H,192,232)(H,193,233)(H,194,239)(H,195,234)(H,196,227)(H,197,243)(H,198,242)(H,199,240)(H,200,244)(H,201,220)(H,202,228)(H,203,229)(H,204,238)(H,213,214)(H,215,216)(H4,161,162,171)(H4,163,164,172)(H4,165,166,173)(H4,167,168,174)/t80-,81-,82-,83-,84-,85-,86+,94-,95-,96-,97-,98-,99-,100-,101-,102-,103-,104-,105-,106-,107-,108-,109-,110-,111-,112-,113-,114-,120-,121-,122-,123-/m0/s1

InChI Key

MEFNIEDWNSBZSR-UCRGYRMUSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CC1=CC=CC=C1)C(=O)NC(C(C)O)C(=O)NC(CO)C(=O)NC(CO)C(=O)NC(CC2=CC=C(C=C2)O)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(C(C)CC)C(=O)NC(CC(C)C)C(=O)NCC(=O)NC(CCC(=O)N)C(=O)NC(CC(C)C)C(=O)NC(CC3=CC=C(C=C3)O)C(=O)NC(C)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCCN)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(CC4=CNC=N4)C(=O)NC(CCC(=O)O)C(=O)NC(C(C)CC)C(=O)NC(CCSC)C(=O)NC(CC(=O)N)C(=O)NC(CCCNC(=N)N)C(=O)N)NC(=O)C(C)NC(=O)C(CC(=O)O)NC(=O)C(C)NC(=O)C(CC5=CNC=N5)N

1. Proteolytic degradation of rat growth hormone-releasing factor(1-29) amide in rat pituitary and hypothalamus

L Boulanger, C Lazure, L Lefrançois, P Gaudreau Brain Res. 1993 Jul 9;616(1-2):39-47. doi: 10.1016/0006-8993(93)90189-t.

The identification of peptide bonds vulnerable to tissue peptidases is a valuable approach to design peptide agonists which exhibit a longer duration of action than the native molecules. Therefore, the kinetic of disappearance of rat growth hormone-releasing factor (rGRF(1-29)NH2) and the identification of its metabolites were studied in rat pituitary and hypothalamus. Synthetic rGRF(1-29)NH2 (10 microM) was incubated (0-120 min, 37 degrees C) in the presence of a pituitary (237 +/- 51 micrograms protein/ml) or hypothalamus homogenate (576 +/- 27 micrograms protein/ml). Using analytical high pressure liquid chromatography (HPLC), apparent half-lives of 22 +/- 3 min and 25 +/- 4 min were found in pituitary and hypothalamus, respectively. In both tissues, three degradation products, all less hydrophobic than the native peptide, were detected and isolated by preparative HPLC. The identification of the purified metabolites was ascertained by amino acid analysis, sequencing and chromatography with synthetic homologs. These results indicate that the main sites of cleavage in the pituitary and hypothalamus are Lys21-Leu22 (trypsin-like cleavage site), Leu14-Gly15 and Tyr10-Arg11 (chymotrypsin-like cleavage sites). TLCK and leupeptin did not affect the formation of fragment (1-21)OH while TPCK blocked the cleavage of Leu14-Gly15. The low affinity of fragment (1-21)NH2 for pituitary GRF binding sites suggests that hydrolysis of the Lys21-Leu22 bond inactivates rGRF(1-29)NH2 in this target tissue.

2. Catabolism of rat growth hormone-releasing factor(1-29) amide in rat serum and liver

L Boulanger, P Roughly, P Gaudreau Peptides. 1992 Jul-Aug;13(4):681-9. doi: 10.1016/0196-9781(92)90173-z.

Clinical and veterinary uses of growth hormone-releasing factor [GRF(1- 29)NH2] require the design of analogs that are resistant to proteolysis by serum and liver degrading enzymes. This study investigated rat GRF(1-29)NH2 processing in serum and liver homogenate by means of high pressure liquid chromatography (HPLC). Synthetic rGRF(1-29)NH2 (30 microM) was incubated (0-120 min, 37 degrees C) in serum (49 +/- 8 mg prot./ml). The rGRF(1-29)NH2 (10 microM) was also incubated (0-120 min, 37 degrees C) with liver homogenate (200 +/- 6 micrograms prot./ml). Time course studies of rGRF(1-29)NH2 disappearance showed apparent half-lives of 18 +/- 4 min and 13 +/- 3 min in serum and liver homogenate, respectively. This was accompanied by the appearance of degradation products that were all less hydrophobic than the native peptide. In the serum, two major metabolites were detected and isolated by preparative HPLC. Combined results of amino acid analysis, sequencing, and chromatography with synthetic homologs revealed the presence of rGRF(1-20)OH and (3-20)OH. A small amount of rGRF(12-29)NH2, coeluting with rGRF(3-20)OH, was also found by sequencing. In the liver, rGRF(1-18)OH, (3-18)OH, and (1-10)OH were identified. The peptide bond Ala2-Asp3 (DPP IV cleavage site) was hydrolyzed in both serum and liver. Other tissue-specific cleavage sites were Arg11-Arg12 and Arg20-Lys21 (trypsin-like cleavage site) in the serum, and Tyr10-Arg11 and Tyr18-Ala19 (chymotrypsin-like cleavage site) in the liver.(ABSTRACT TRUNCATED AT 250 WORDS)

3. Structural requirements for the activation of rat anterior pituitary adenylate cyclase by growth hormone-releasing factor (GRF): discovery of (N-Ac-Tyr1, D-Arg2)-GRF(1-29)-NH2 as a GRF antagonist on membranes

P Robberecht, D H Coy, M Waelbroeck, M L Heiman, P de Neef, J C Camus, J Christophe Endocrinology. 1985 Nov;117(5):1759-64. doi: 10.1210/endo-117-5-1759.

The efficacy and potency of 14 GH-releasing factor (GRF) analogs, substituted in position 1 to 7, on adenylate cyclase activation in crude homogenates from rat anterior pituitary were related to those of human pancreatic GRF(1-29)-amide and vasoactive intestinal peptide. Among several D-amino acid substitutions, that in position 2 was the only one to yield a super-agonist [with a Kact (concentration required for half-maximal adenylate cyclase activation) 2 times lower than that of GRF(1-29)-NH2]. By contrast, D-isomer substitution in position 1 and 3 was without effect and D-isomer substitution in position 4, 6, or 7 decreased the affinity of the analog. The N-acetylated analog of GRF was as potent and active as the parent peptide, and the identity of the amino acid in position 2 of (N-Ac-Tyr1)-GRF(1-29)-NH2 proved to be determining for enzyme activation, with D-Phe2 and D-Trp2 derivatives acting as partial agonists and the (N-Ac-Tyr1,D-Arg2) analog being an efficient competitive antagonist of GRF(1-29)-NH2. With use of this antagonist, it was possible to demonstrate that GRF and vasoactive intestinal peptide receptors represent distinct entities in the rat anterior pituitary.