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(3-Mercaptopropyl)ammonium chloride, also known as APT, is an organosulfur compound that features a mercaptopropyl group attached to an ammonium ion. It is known for its unique chemical properties and potential applications in various fields.

7211-54-3

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7211-54-3 Usage

Uses

Used in High-Speed Switching Devices:
(3-Mercaptopropyl)ammonium chloride is used as a material to form a plasmonic tunneling gap through Coulomb blockage, which can potentially be utilized in high-speed switching devices. This application takes advantage of its ability to create a gap that allows for rapid switching of electrical signals.
Used in Photovoltaic and Photo-Sensor Devices:
In the photovoltaic industry, (3-Mercaptopropyl)ammonium chloride is used as a self-assembled monolayer (SAM) on gold nanorods (AuNR). This application is for controlled spacing and photon absorption, which can enhance the efficiency and performance of photovoltaic and other photo-sensors based devices. The formation of a SAM on AuNR allows for precise control over the spacing between the nanorods, which in turn affects their optical and electronic properties.

Check Digit Verification of cas no

The CAS Registry Mumber 7211-54-3 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,2,1 and 1 respectively; the second part has 2 digits, 5 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 7211-54:
(6*7)+(5*2)+(4*1)+(3*1)+(2*5)+(1*4)=73
73 % 10 = 3
So 7211-54-3 is a valid CAS Registry Number.
InChI:InChI=1/C3H9NS.ClH/c4-2-1-3-5;/h5H,1-4H2;1H

7211-54-3 Well-known Company Product Price

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  • Aldrich

  • (739294)  3-Amino-1-propanethiol hydrochloride  technical grade

  • 7211-54-3

  • 739294-250MG

  • 3,181.23CNY

  • Detail
  • Aldrich

  • (739294)  3-Amino-1-propanethiol hydrochloride  technical grade

  • 7211-54-3

  • 739294-500MG

  • 5,412.42CNY

  • Detail

7211-54-3SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name (3-mercaptopropyl)ammonium chloride

1.2 Other means of identification

Product number -
Other names 3-Amino-1-propanethiolHCl

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:7211-54-3 SDS

7211-54-3Relevant academic research and scientific papers

Design and Synthesis of Simplified Largazole Analogues as Isoform-Selective Human Lysine Deacetylase Inhibitors

Reddy, Damodara N.,Ballante, Flavio,Chuang, Timothy,Pirolli, Adele,Marrocco, Biagina,Marshall, Garland R.

supporting information, p. 1613 - 1633 (2016/03/05)

Selective inhibition of KDAC isoforms while maintaining potency remains a challenge. Using the largazole macrocyclic depsipeptide structure as a starting point for developing new KDACIs with increased selectivity, a combination of four different simplified largazole analogue (SLA) scaffolds with diverse zinc-binding groups (for a total of 60 compounds) were designed, synthesized, and evaluated against class I KDACs 1, 3, and 8, and class II KDAC6. Experimental evidence as well as molecular docking poses converged to establish the cyclic tetrapeptides (CTPs) as the primary determinant of both potency and selectivity by influencing the correct alignment of the zinc-binding group in the KDAC active site, providing a further basis for developing new KDACIs of higher isoform selectivity and potency.

ISOFORM-SELECTIVE LYSINE DEACETYLASE INHIBITORS

-

Paragraph 0100; 0103, (2016/11/21)

Isoform-selective lysine deacetylase inhibitors are described. Inhibitors of the lysine deacetylase enzyme are useful as antitumor drugs and for treating addiction, asthma, cardio-vascular disease, immunosuppression, neurodegenerative diseases, sepsis, sickle-cell disease, uveal melanoma and termination of viral latency, particularly HIV-1 latency.

PROTEIN KINASE D INHIBITORS

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Page/Page column 52-53, (2012/06/30)

Compounds according to Formula (I), are potent inhibitors of protein kinase D (pan-PKD) activity. PKD controls key signaling cascades in cells, affecting cell proliferation, gene transcription, and protein trafficking. Accordingly, pharmaceutically acceptable compositions of the inventive compounds are candidate therapeutics for pathological conditions conditioned by changes in PKD activity.

Synthesis and structure-activity relationships of benzothienothiazepinone inhibitors of protein kinase D

Bravo-Altamirano, Karla,George, Kara M.,Frantz, Marie-Celine,Lavalle, Courtney R.,Tandon, Manuj,Leimgruber, Stephanie,Sharlow, Elizabeth R.,Lazo, John S.,Wang, Q. Jane,Wipf, Peter

scheme or table, p. 154 - 159 (2011/04/15)

Protein kinase D (PKD) is a member of a novel family of serine/threonine kinases that regulate fundamental cellular processes. PKD is implicated in the pathogenesis of several diseases, including cancer. Progress in understanding the biological functions and therapeutic potential of PKD has been hampered by the lack of specific inhibitors. The benzoxoloazepinolone CID755673 was recently identified as the first potent and selective PKD inhibitor. The study of structure-activity relationships (SAR) of this lead compound led to further improvements in PKD1 potency. We describe herein the synthesis and biological evaluation of novel benzothienothiazepinone analogues. We achieved a 10-fold increase in the in vitro PKD1 inhibitory potency for the second generation lead kb-NB142-70 and accomplished a transition to an almost equally potent novel pyrimidine scaffold, while maintaining excellent target selectivity. These promising results will guide the design of pharmacological tools to dissect PKD function and pave the way for the development of potential anticancer agents.

Reversible inactivation of bovine plasma amine oxidase by cysteamine and related analogs

Jeon, Heung Bae,Jang, Yujin

experimental part, p. 442 - 446 (2011/10/12)

Cysteamine (1) was reported many years ago to reversibly inhibit lentil seedling amine oxidase, through the formation of a complex with thioacetaldehyde, the turnover product of 1. Herein, cysteamine (1) and its analogs 2-(methylamino)ethanethiol (3) and 3-aminopropanethiol (6) were found to be reversible inhibitors of bovine plasma amine oxidase (BPAO), but 2-(methylthio)ethylamine (7) was determined to be a weak irreversible inhibitor of BPAO. Based on our results, indicating the necessity of a sulfhydryl-amine for reversible inactivation of BPAO, the failure of inhibited BPAO to recover activity after gel filtration, the first-order kinetics of activity recovery upon dialysis, and 2,4,6-trihydroxyphenylalanine quinine (TPQ) cofactor transformation which indicated from the results of phenylhydrazine titration and substrate protection, we propose a mechanism for the reversible inactivation of BPAO by 1 involving the formation of a cofactor adduct, thiazolidine, between BPAO and 1.

Synthesis of guanosine and deoxyguanosine phosphoramidites with cross-linkable thioalkyl tethers for direct incorporation into RNA and DNA

Hou, Xiaorong,Wang, Gang,Gaffney, Barbara L.,Jones, Roger A.

experimental part, p. 1076 - 1094 (2010/09/05)

We describe the synthesis of protected phosphoramidites of deoxyriboguanosine and guanosine derivatives containing a thiopropyl tether at the guanine N2 (7a,b) for site-specific crosslinking from the minor groove of either DNA or RNA to a thiol of a prote

One-pot preparation of coenzyme a analogues via an improved chemo-enzymatic synthesis of pre-CoA thioester synthons

Van Wyk, Marianne,Strauss, Erick

, p. 398 - 400 (2007/10/03)

Coenzyme A analogues are synthesized in a one-pot preparation by biotransformation of pantothenate thioesters through the simultaneous use of three CoA biosynthetic enzymes, followed by aminolysis. The Royal Society of Chemistry.

Synthesis of novel S-bridged heterotrinuclear complexes containing six-membered chelate rings: Structural, spectroscopic, and electrochemical properties of [Co{Rh(apt)3}2]3+ (apt = 3-aminopropanethiolate)

Amir, Nagina,Motonishi, Masaru,Fujita, Mitsuharu,Miyashita, Yoshitaro,Fujisawa, Kiyoshi,Okamoto, Ken-Ichi

, p. 1041 - 1049 (2007/10/03)

A bidentate ligand, 3-aminopropanethiolate (apt), was synthesized and treated with RhCl3·3H2O in basic water to yield a novel mononuclear complex, fac(S)-[Rh(apt)3] (1), which was characterized by spectroscopic methods. Furthermore, the reaction of 1 with CoCl2·6H2O in water formed the linear-type, S-bridged trinuclear complexes ΔΛ-[Co{Rh(apt)3} 2]3+ (2a) and ΔΔ/ΛΛ-[Co{Rh(apt) 3}2]3+ (2b), which were characterized by stereochemical, spectrochemical, and electrochemical methods. 2a and 2b are stable and exhibit trivalency in water. X-ray crystallographic analysis of 2a and 2b showed that all of the bridging sulfur atoms are fixed in the R configuration for the Δ unit and in the S configuration for the Λ unit, and each complex has six six-membered chelate rings, all of which are in the chair conformation. The crystal structure of the corresponding 2-aminoethanethiolate (aet) trinuclear complex ΔΛ-[Co{Rh(aet) 3}2]3+ (4a) was also determined. The structures of 2a and 2b have some differences from that of 4a as a result of the six-membered chelate rings. The Co...Rh distances in 2a and 2b [3.0490(4) and 3.063(1) A] are significantly longer than this distance in the aet complex 4a [2.9139(2) A]. The UV/Vis absorption spectra of 2a and 2b indicate a shift to higher energies as compared with 4a and ΔΔ/ ΛΛ-[Co{Rh(aet)3}2]3+ (4b). The chemical shifts for the NCH2 and SCH2 carbon atoms in 2a and 2b are shifted to higher fields than those for 4a and 4b in the NMR spectra. The CoIII/II redox potential values are -0.56 V (2a) and -0.57 V (2b) compared with -0.35 V (4a) and -0.36 V (4b). This shows that the Co III state is more stable in 2a and 2b than it is in 4a and 4b. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.

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