1.Molecular conformation of achatin-I, an endogenous neuropeptide containing D-amino acid residue. X-ray crystal structure of its neutral form.
Kamatani Y1, Minakata H, Iwashita T, Nomoto K, In Y, Doi M, Ishida T. FEBS Lett. 1990 Dec 10;276(1-2):95-7.
The molecular conformation of achatin-I neutral form (H-Gly-D-Phe-Ala-Asp-OH), an endogenous neuropeptide, was elucidated by X-ray crystal analysis. The molecule has a type II' beta-turn structure with the D-Phe-Ala residues at the corner of the bend, which is further stabilized by two NH(Gly)...C gamma = O sigma(Asp) and NH(Asp)...C gamma = O sigma(Asp) intramolecular hydrogen bonds. This turn conformation may be an important feature of achatin-I related to its neuroexcitatory activity.
2.Isolation and identification of paralytic peptides from hemolymph of the lepidopteran insects Manduca sexta, Spodoptera exigua, and Heliothis virescens.
Skinner WS1, Dennis PA, Li JP, Summerfelt RM, Carney RL, Quistad GB. J Biol Chem. 1991 Jul 15;266(20):12873-7.
Seven paralytic peptides were isolated and identified from lepidopteran hemolymph. All of these peptides cause rapid, rigid paralysis when injected into Manduca sexta and some other lepidopteran larvae. Each peptide contains 23 amino acid residues including 2 cysteines and the carboxyl termini are acidic. Synthetic peptides in the disulfide or reduced forms, and as carboxyl-terminal acids or amides were equally paralytic. The most potent paralytic peptide, Mas PP I, has the following sequence: H-Glu-Asn-Phe-Ala-Gly-Gly-Cys-Ala-Thr-Gly-Tyr-Leu- Arg-Thr-Ala-Asp-Gly-Arg-Cys-Lys-Pro-Thr-Phe-OH. The two peptides from M. sexta hemolymph are remarkable in that they are autoparalytic (i.e. factors in collected hemolymph that are paralytic when injected into the same larvae).
3.Adsorption and photocatalytic decomposition of amino acids in TiO2 photocatalytic systems.
Tran TH1, Nosaka AY, Nosaka Y. J Phys Chem B. 2006 Dec 21;110(50):25525-31.
The adsorption and photodecomposition of seven kinds of amino acids on a TiO2 surface were investigated by zeta potential measurements and 1H NMR spectroscopy in TiO2 aqueous suspension systems. The decomposition rates increased in the order of Phe < Ala < Asp < Trp < Asn < His < Ser. For Phe, Trp, Asn, His, and Ser, the isoelectric point (IEP) of TiO2 shifted to a lower pH with increasing decomposition rates upon adsorption on TiO2, suggesting that the effective adsorption and photocatalytic sites for these amino acids should be the basic terminal OH on the solid surface. Since the amino acids that decomposed faster than the others contain -OH (Ser), -NH (Trp, His), or -NH2 (Asn) in their side chain, they are considered to interact with the basic terminal OH groups more preferably by the side chain and are vulnerable to photocatalytic oxidation. On the other hand, Ala interacts with the acidic bridged OH on TiO2 to cause an IEP shift to a higher pH.
4.Isolation and primary structure of the eclosion hormone of the tobacco hornworm, Manduca sexta.
Kataoka H, Troetschler RG, Kramer SJ, Cesarin BJ, Schooley DA. Biochem Biophys Res Commun. 1987 Jul 31;146(2):746-50.
Eclosion hormone was isolated from trimmed pharate adult heads of Manduca sexta by an eight step purification procedure using a Heliothis virescens in vivo bioassay. The neuropeptide was active in second stadium M. sexta. The primary structure was determined by sequence analyses of the intact peptide and fragment peptides generated by lysyl endopeptidase, endoproteinase Glu-C, and proline-specific endopeptidase. The nature of the carboxyl terminus as a free acid was elucidated by analysis of amino acids from digestion of the intact peptide with lysyl endopeptidase, which liberated leucine, but no leucine amide. The complete primary structure of M. sexta closion hormone is H-Asn-Pro-Ala-Ile-Ala-Thr-Gly-Tyr-Asp-Pro-Met-Glu-Ile-Cys-Ile-Glu-Asn-Cy s-Ala- Gln-Cys-Lys-Lys-Met-Leu-Gly-Ala-Trp-Phe-Glu-Gly-Pro-Leu-Cys-Ala-Glu-Ser- Cys-Ile Lys-Phe-Lys-Gly-Lys-Leu-Ile-Pro-Glu-Cys-Glu-Asp-Phe-Ala-Ser-Ile-Ala-Pro- Phe-Leu-Asn-Lys-Leu-OH.
