L-β-Homophenylalanine
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L-β-Homophenylalanine

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Category
β−Amino acids
Catalog number
BAT-006886
CAS number
26250-87-3
Molecular Formula
C10H13NO2
Molecular Weight
179.20
L-β-Homophenylalanine
IUPAC Name
(3S)-3-amino-4-phenylbutanoic acid
Synonyms
H-Phe-(C#CH2)OH; H-β-homoPhe-OH; (S)-3-Amino-4-phenylbutanoic acid
Purity
95%
Density
1.164 g/cm3
Melting Point
207 °C
Boiling Point
324.8°C at 760 mmHg
Storage
Store at 2-8 °C
InChI
InChI=1S/C10H13NO2/c11-9(7-10(12)13)6-8-4-2-1-3-5-8/h1-5,9H,6-7,11H2,(H,12,13)/t9-/m0/s1
InChI Key
OFVBLKINTLPEGH-VIFPVBQESA-N
Canonical SMILES
C1=CC=C(C=C1)CC(CC(=O)O)N
1. Synthesis of Optically Active beta-Amino Acid N-Carboxyanhydrides
J Cheng, JW Ziller, TJ Deming Org Lett. 2000 Jun 29;2(13):1943-1946. doi: 10.1021/ol000122w.
Methodology has been developed for the general synthesis of optically active beta-amino acid N-carboxyanhydrides (beta-NCAs) through cyclization of N(beta)-Boc or N(beta)-Cbz beta-amino acids using phosphorus tribromide. The formation of beta-NCAs was confirmed by spectroscopy as well as an X-ray structural determination of beta-homoalanine-N-carboxyanhydride. The beta-NCA molecules could be polymerized in good yield to give optically active poly(beta-peptides) that adopt stable chiral conformations in solution. For example, helical oligo(L-beta-homophenylalanine) was synthesized by polymerization of L-beta-homophenylalanine-N-carboxyanhydride.
2. Analogues of arginine vasopressin and its agonist and antagonist modified in the N-terminal part of the molecule with l-beta-homophenylalanine
D Sobolewski, W Kowalczyk, A Prahl, I Derdowska, J Slaninová, J Zabrocki, B Lammek J Pept Res. 2005 Apr;65(4):465-71. doi: 10.1111/j.1399-3011.2005.00238.x.
In continuation of our efforts to elucidate the role of positions 2 and 3 in arginine vasopressin (AVP) and its analogues, we designed and synthesized peptides modified in these positions with l-beta-homophenylalanine (beta-Hph). Two of them had just this single modification, the next two peptides are analogues of the V2 agonist, namely [3-mercaptopropionic acid (Mpa)1]AVP (dAVP). The last two compounds were designed by substitution of positions 2 or 3 of a potent V(1a) antagonist, [1-mercaptocyclohexaneacetic acid (Cpa)1]AVP, with beta-Hph. All the peptides were tested for their pressor and antidiuretic and uterotonic in vitro activities in the rat. All the activities tested have been found to be significantly decreased. Three analogues, i.e. [Mpa(1),beta-Hph2]AVP, [Cpa1,beta-Hph2]AVP, [Cpa1,beta-Hph3]AVP, turned out to be uterotonic antagonists with pA2 = 6.3 +/- 0.2, 6.3 +/- 0.1, 6.0 +/- 0.3 respectively. The last one exhibited antipressor properties also (pA2 = 6.4 +/- 0.1).
3. Major Factors for the Persistent Folding of Hybrid α, β, γ-Hybrid Peptides Into Hairpins
Yulong Zhong, Quan Tang, Daniel P Miller, Eva Zurek, Rui Liu, Zhong-Lin Lu, Bing Gong Front Chem. 2020 Sep 29;8:530083. doi: 10.3389/fchem.2020.530083. eCollection 2020.
Factors responsible for the persistent adoption of hairpin conformations by hybrid oligopeptides, each having a central β/α dipeptide segment flanked by aromatic γ-amino acid (γAr) residues, are probed. Our recent studies revealed that tetrapeptide 1 and 2, having central dipeptide segments consisting of β-alanine (β-Ala) and glycine (Gly), and L-β-homophenylalanine (L-β-homoPhe) and Gly residues, respectively, that are flanked by γAr residues, fold into well-defined, expanded β-turns with doubly H-bonded γAr residues. Replacing the γAr residues of 1 and 2 with L-Val and L-Leu residues results in tetrapetides 1 ' and 2 ' that fail to fold into defined conformations, which confirms the decisive role played by the H-bonded γAr residues in the promoting folding of 1 and 2. Attaching L-Val and L-Leu residues to the termini of 1 affords hexapeptide 1a. With an additional H-bond between its L-Val and L-Leu residues, peptide 1a folds into a hairpin with higher stability than that of 1, indicating that the expanded β-turn can nucleate and stabilize β-hairpin with longer β-strands. Attaching L-Val and L-Leu residues to the termini of 2 affords hexapeptide 2a. Substituting the L-β-homoPhe residue of 2a with a D-β-homoPhe residue gives hexapeptide 2b. Surprisingly, hexapeptide 2a fold into a hairpin showing the similar stability as those of tetrapeptides 1 and 2. Hexapeptide 2b, with its combination of a D-β-homoPhe residue and the L-Val/L-Leu pair, fold into a hairpin that is significantly more stable than the other hybrid peptides, demonstrating that a combination of hetero-chirality between the β-amino acid residue of the dipeptide loop and the α-amino acid residues of the β-strands enhances the stability of the resultant β-hairpin.
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