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Angiotensin I (human, mouse, rat)

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

Angiotensin 1 (Human), an endogenous peptide substrate for angiotensin converting enzyme (ACE), is precursor to the vasoconstrictor peptide angiotensin II.

Category

Peptide Inhibitors

Catalog number

BAT-010541

CAS number

484-42-4

Molecular Formula

C62H89N17O14

Molecular Weight

1296.48

Specification
Reference Reading

IUPAC Name

(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoic acid

Synonyms

Angiotensin 1 Human; H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-OH; L-alpha-aspartyl-L-arginyl-L-valyl-L-tyrosyl-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanyl-L-histidyl-L-leucine; Pepsitensin; Proangiotensin; 5-Ile-angiotensin I; 5-L-Isoleucine-angiotensin I

Appearance

White or Off-white Lyophilized Powder

Purity

≥95%

Density

1.43±0.1 g/cm3

Boiling Point

1441.1±75.0°C at 760 mmHg

Sequence

DRVYIHPFHL

Storage

Store at -20°C

Solubility

Soluble in Water, DMSO

InChI

1S/C62H89N17O14/c1-7-35(6)51(78-56(87)44(25-37-17-19-40(80)20-18-37)74-58(89)50(34(4)5)77-53(84)42(15-11-21-68-62(64)65)71-52(83)41(63)28-49(81)82)59(90)75-46(27-39-30-67-32-70-39)60(91)79-22-12-16-48(79)57(88)73-43(24-36-13-9-8-10-14-36)54(85)72-45(26-38-29-66-31-69-38)55(86)76-47(61(92)93)23-33(2)3/h8-10,13-14,17-20,29-35,41-48,50-51,80H,7,11-12,15-16,21-28,63H2,1-6H3,(H,66,69)(H,67,70)(H,71,83)(H,72,85)(H,73,88)(H,74,89)(H,75,90)(H,76,86)(H,77,84)(H,78,87)(H,81,82)(H,92,93)(H4,64,65,68)/t35-,41-,42-,43-,44-,45-,46-,47-,48-,50-,51-/m0/s1

InChI Key

ORWYRWWVDCYOMK-HBZPZAIKSA-N

Canonical SMILES

CCC(C)C(C(=O)NC(CC1=CN=CN1)C(=O)N2CCCC2C(=O)NC(CC3=CC=CC=C3)C(=O)NC(CC4=CN=CN4)C(=O)NC(CC(C)C)C(=O)O)NC(=O)C(CC5=CC=C(C=C5)O)NC(=O)C(C(C)C)NC(=O)C(CCCN=C(N)N)NC(=O)C(CC(=O)O)N

1.Nitric oxide modulates captopril-mediated angiotensin-converting enzyme inhibition in porcine iliac arteries.

Persson K;Andersson RG Eur J Pharmacol. 1999 Nov 26;385(1):21-7.

The influence of the angiotensin-converting enzyme inhibitor captopril on bradykinin-and angiotensin I-induced responses with special regard to nitric oxide (NO) was studied. Auxometric tension and angiotensin-converting enzyme activity was studied in isolated porcine iliac arteries. Captopril potentiated bradykinin-induced contraction of preparations with intact endothelium; this potentiation was not seen with the kininase I inhibitor mergepta or a bradykinin B(1)-receptor antagonist. Captopril did not affect bradykinin-induced relaxation. The captopril-mediated increase of bradykinin-induced contraction was only seen in preparations with intact endothelium, while captopril did not affect arterial strips treated with Nomega-nitro-L-arginine. Angiotensin I-induced contractions was less reduced by captopril when the strips were pretreated with Nomega-nitro-L-arginine. Both captopril and the NO donor S-nitroso-N-acetyl-penicillamine inhibited angiotensin-converting enzyme activity. An additional reduction in angiotensin-converting enzyme activity was seen when S-nitroso-N-acetyl-penicillamine was added to captopril-treated preparations. In conclusion, captopril increased bradykinin-induced contraction in a NO-dependent manner.

2.Transepithelial transport of milk-derived angiotensin I-converting enzyme inhibitory peptide with the RLSFNP sequence.

Guo Y;Gan J;Zhu Q;Zeng X;Sun Y;Wu Z;Pan D J Sci Food Agric. 2018 Feb;98(3):976-983. doi: 10.1002/jsfa.8545. Epub 2017 Sep 8.

BACKGROUND: ;To exert an antihypertensive effect after oral administration, angiotensin I-converting enzyme (ACE)-inhibitory peptides must remain active after intestinal transport. The purpose of this article is to elucidate the transport permeability and route of ACE-inhibitory peptide Arg-Leu-Ser-Phe-Asn-Pro (RLSFNP) across the intestinal epithelium using Caco-2 cell monolayers.;RESULTS: ;Intact RLSFNP and RLSFNP breakdown fragments F, FNP, SFNP and RLSF were found in RLSFNP transport solution across Caco-2 cell monolayers using ultra-performance liquid chromatography-tandem mass spectrometry. RLSFNP fragments FNP, SFNP and RLSF also contributed to ACE inhibitory effects. Protease inhibitors (bacitracin and leupeptin) and absorption enhancers (sodium glycocholate hydrate, sodium deoxycholate and Na;2; EDTA) improved the transport flux of RLSFNP. A transport inhibitor experiment showed that intact RLSFNP may be transported via the paracellular route.;CONCLUSION: ;Intact RLSFNP can be transported across the Caco-2 cell monolayers via the paracellular route. Extensive hydrolysis was the chief reason for the low permeability of RLSFNP. © 2017 Society of Chemical Industry.;© 2017 Society of Chemical Industry.

3.Marked ion dependence of 125I-angiotensin I binding to atypical sites on Mycoplasma hyorhinis.

Smith RD Peptides. 1999;20(2):165-9.

125I-Ang I binding to atypical sites on Mycoplasma hyorhinis-contaminated IEC-18 cell membranes increased with increasing pH and [NaCl] (ED50 at 500 mM; maximal 13-fold increase at 2 M NaCl). Alkali metal chlorides and sodium halides increased binding with rank orders of Na+ < K+ < Rb+ < Cs+ = Li+ and F- < Cl- < Br < I. Covalent cross-linking of 125I-Ang I labeled a discrete band of 97 kDa. These findings suggest that the site is not a G protein-coupled receptor, but may play a role in the sensing by Mycoplasma of the ionic composition and/or pH of its environment.