4512-32-7

Basic information

• Product Name: ALPHA-AMINOISOBUTYRIC ACID T-BUTYL ESTER
• Synonyms: ALPHA-AMINOISOBUTYRIC ACID T-BUTYL ESTER;ALPHA-METHYLALANINE T-BUTYL ESTER;H-AIB-OTBU;H-Aib-OtBu·HCl(α-AMinoisobutyric acid tert-butyl ester);2-Amino-2-methylpropionic acid tert-butyl ester;tert-Butyl 2-amino-2-methylpropanoate;H-a-Me-Ala-OtBu · HCl;tert-Butyl 2-aMinoisobutyrate hydrochloride, 98%
• CAS NO: 4512-32-7
• Molecular Formula: C₈H₁₇NO₂
• Molecular Weight: 159.23
• EINECS: 1533716-785-6
• Mol File: 4512-32-7.mol

Chemical Properties

• Boiling Point: 180℃
• Flash Point: 53℃
• Appearance: White/Powder
• Density: 0.948
• Storage Temp.: Store at 0°C
• PKA: 7.98±0.25(Predicted)
• CAS DataBase Reference: ALPHA-AMINOISOBUTYRIC ACID T-BUTYL ESTER(CAS DataBase Reference)
• NIST Chemistry Reference: ALPHA-AMINOISOBUTYRIC ACID T-BUTYL ESTER(4512-32-7)
• EPA Substance Registry System: ALPHA-AMINOISOBUTYRIC ACID T-BUTYL ESTER(4512-32-7)

Safety Data

• Hazardous Substances Data: 4512-32-7(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Upstream product

• 1355158-73-4 tert-butyl 2-(benzylamino)-2-methylpropanoate 
• 23877-12-5 tert-butyl bromoisobutyrate 
• 4512-31-6 benzyloxycarbonyl-α-aminoisobutyric acid tert-butyl ester 
• 62-57-7 2-Aminoisobutyric acid 
• 75-65-0 tert-butyl alcohol 
• 540-88-5 acetic acid tert-butyl ester 

Downstream Products

• 84758-64-5 Z-L-Val-Aib-OtBu 
• 97444-24-1 benzyloxycarbonyl-α-methylalanyl-d6-α-methylalanyl-α-methylalanine t-butyl ester 
• 503564-51-0 Z-L-(αMe)Val-Aib-OtBu 
• 854055-62-2 Z-L-Tle-Aib-OtBu 
• 134269-29-7 Z-Gly-Aib-OBu^t 
• 93-91-4 1-phenylbutan-1,3-dione 
• 1174062-37-3 Z-L-AlaT-Aib-OtBu 
• 1164339-07-4 4-[(S)-4-carboxy-2-({5-[(1-carboxy-1-methylethyl)carbamoylmethoxy]-1-phenyl-1H-pyrazole-3-carbonyl}amino)butyryl]piperazine-1-carboxylic acid ethyl ester trifluoroacetate 

Relevant articles and documents

Direct observation of intramolecular hydrogen bonds in peptide 3 10 helices by 3hJN,C′ scalar couplings

Differentiating helices: The direct observation of hydrogen bonds by 3hJN,C′ scalar couplings (see picture) is not only possible for α-helix and β-sheet peptides and proteins, but for 310-helical peptides as well. The meth

First interchain peptide interaction detected by ESR in fully synthetic, template-assisted, two-helix bundles

We have designed and synthesized by solution methods two simple two-helix bundles based on a conformationally constrained cyclo-dipeptide template to the side chains of which two short, 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin-monolabeled, 310-helical peptides are covalently tethered. The preferred conformation of the appended chains has been assessed by FTIR absorption. The conclusions are corroborated by an X-ray diffraction analysis of one of the terminally blocked pentapeptide tails. For the first time, a solvent-dependent, inter-helix interaction has been monitored by conventional ESR spectroscopy on fully synthetic peptide systems. Half-field ESR measurements of these side-chain-substituted templates provided an experimental average distance between the two labels that is in good accord with that determined in a molecular modeling study.

NOVEL POLYMORPH FORM OF ( R)-2-[2-AMINO-3-(INDOL-3-YL)PROPIONYLAMINO]-2-METHYLPROPIONIC ACID AND USES THEREOF

This invention relates to a novel polymorph form of compound (R)-2-[2-amino-3-(indol-3- yl)propionylamino]-2-methylpropionic acid, a process for making the novel polymorph form of the compound, and uses thereof for making other polymorph forms of the compound. The invention further relates to composition comprising novel polymorph form of the compound and a pharmaceutically acceptable carrier or excipient.

Dipeptide analogs for treating conditions associated with amyloid fibril formation

Dipeptide analogs comprising a tryptophan (Trp) moiety coupled to a beta-sheet breaker moiety derived from alpha-aminoisobutyric acid (Aib) are disclosed. The dipeptide analogs exhibit an improved performance in inhibiting amyloid fibril formation, as compared to previously described dipeptides. Compositions containing the dipeptide analogs and uses thereof in treating amyloid-associated diseases and disorders are also disclosed.

Deracemization and the first CD spectrum of a 310-helical peptide made of achiral α-amino-isobutyric acid residues in a chiral membrane mimetic environment

Interaction of the racemic helical homo-octapeptide made by the achiral Cα-methyl alanine (Aib) amino acid with a chiral enantiopure micellar aggregate made of N-dodecylproline led to the deracemization of the helical Aib sequence thus allowing

Trichogin GA IV: A versatile template for the synthesis of novel peptaibiotics

Trichogin GA IV, isolated from the fungus Trichoderma longibrachiatum, is the prototype of lipopeptaibols, the sub-class of short-length peptaibiotics exhibiting membrane-modifying properties. This peptaibol is predominantly folded in a mixed 310-/α-helical conformation with a clear, albeit modest, amphiphilic character, which is likely to be responsible for its capability to perturb bacterial membranes and to induce cell death. In previous papers, we reported on the interesting biological properties of trichogin GA IV, namely its good activity against Gram positive bacteria, in particular methicillin-resistant S. aureus strains, its stability towards proteolytic degradation, and its low hemolytic activity. Aiming at broadening the antimicrobial activity spectrum by increasing the peptide helical amphiphilicity, in this work we synthesized, by solution and solid-phase methodologies, purified and fully characterized a set of trichogin GA IV analogs in which the four Gly residues at positions 2, 5, 6, 9, lying in the poorly hydrophilic face of the helical structure, are substituted by one (position 2, 5, 6 or 9), two (positions 5 and 6), three (positions 2, 5, and 9), and four (positions 2, 5, 6, and 9) Lys residues. The conformational preferences of the Lys-containing analogs were assessed by FT-IR absorption, CD and 2D-NMR techniques in aqueous, organic, and membrane-mimetic environments. Interestingly, it turns out that the presence of charged residues induces a transition of the helical conformation adopted by the peptaibols (from 3 10-to α-helix) as a function of pH in a reversible process. The role played in the analogs by the markedly increased amphiphilicity was further tested by fluorescence leakage experiments in model membranes, protease resistance, antibacterial and antifungal activities, cytotoxicity, and hemolysis. Taken together, our biological results provide evidence that some of the least substituted among these analogs are good candidates for the development of new membrane-active antimicrobial agents. The Royal Society of Chemistry 2012.

Toward the selective delivery of chemotherapeutics into tumor cells by targeting peptide transporters: Tailored gold-based anticancer peptidomimetics

Complexes [AuIIIX2(dtc-Sar-AA-O(t-Bu))] (AA = Gly, X = Br (1)/Cl (2); AA = Aib, X = Br (3)/Cl (4); AA = l-Phe, X = Br (5)/Cl (6)) were designed on purpose in order to obtain gold(III)-based anticancer peptidomimetics that might specifically target two peptide transporters (namely, PEPT1 and PEPT2) upregulated in several tumor cells. All the compounds were characterized by means of FT-IR and mono- and multidimensional NMR spectroscopy, and the crystal structure of [AuIIIBr2(dtc-Sar-Aib-O(t- Bu))] (3) was solved and refined. According to in vitro cytotoxicity studies, the Aib-containing complexes 3 and 4 turned out to be the most effective toward all the human tumor cell lines evaluated (PC3, DU145, 2008, C13, and L540), reporting IC50 values much lower than that of cisplatin. Remarkably, they showed no cross-resistance with cisplatin itself and were proved to inhibit tumor cell proliferation by inducing either apoptosis or late apoptosis/necrosis depending on the cell lines. Biological results are here reported and discussed in terms of the structure-activity relationship.

Rational design of gold(III)-dithiocarbamato peptidomimetics for the targeted anticancer chemotherapy

As a further extension of our research work focusing on the development of gold(III)-dithiocarbamato dtc derivatives of oligopeptides as potential anticancer agents, complexes [AuIIIX2(dtc-Sar-l-Ser(t-Bu)- O(t-Bu))] (X = Br (1a)/Cl (

5-(BIPHENYL-4-YL)-3-PHENYL-1,2,4-OXADIAZOLYL DERIVATIVES AS LIGANDS ON THE SPHINGOSINE 1-PHOSPHATE (S1P) RECEPTORS

The present invention provides compounds of Formula (I), as selective S1 P1 inhibitors, as well as their use for treating multiple sclerosis and other diseases.

ENZYME INHIBITORS

Compounds of formula (I), inhibit HDAC activity: wherein A, B and D independently represent =CH- or =N-; W is-CH=CH- Or -CH2CH2-; R1 is a carboxylic acid group (-COOH), or an ester group which is hydrolysable by one or more intracellular carboxylesterase enzymes to a carboxylic acid group; R2 and R3 are selected from the side chains of a natural or non-natural alpha amino acid, provided that neither R2 nor R3 is hydrogen, or R2 and R3, taken together with the carbon to which they are attached, form a 3-6 membered saturated cycloalkyl or heterocyclyl ring; Y is a bond, -C(=O)-, -S(=O)2-, -C(=O)O-, -C(=O)NR'-, -C(=S)-NR', -C(=NH)NR' or -S(=O)2NR - wherein R' is hydrogen or optionally substituted C1-C6 alkyl; L1 is a divalent radical of formula -(Alk1)m(Q)n(Alk2)p- wherein m, n, p, Q, AIk1 and AIk2 are as defined in the claims; X1 represents a bond; -C(=O); or -S(=O)2-; -NR4C(=O)-, -C(=O)NR4-,- NR4C(=O)NR5-, -NR4S(=O)2-, or -S(=O)2NR4- wherein R4 and R5 are independently hydrogen or optionally substituted C1-C6 alkyl; and z is 0 or 1.