• 제목/요약/키워드: Zwitterionic amino acid

검색결과 6건 처리시간 0.021초

Cell Selectivity of an Antimicrobial Peptide Melittin Diastereomer with D-amino Acid in the Leucine Zipper Sequence

  • Zhu, Wan Long;Nan, Yong Hai;Hahm, Kyung-Soo;Shin, Song-Yub
    • BMB Reports
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    • 제40권6호
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    • pp.1090-1094
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    • 2007
  • Melittin (ME), a linear 26-residue non-cell-selective antimicrobial peptide, displays strong lytic activity against bacterial and human red blood cells. To design ME analogue with improved cell selectivity, we synthesized a melittin diastereomer (ME-D) with D-amino acid in the leucine zipper sequence (Leu-6, Lue-13 and Ile-20). Compared to ME, ME-D exhibited the same or 2-fold higher antibacterial activity but 8-fold less hemolytic activity. Circular dichroism analysis revealed that ME-D has much less $\alpha$-helical content in $\alpha$-helical content in the presence of zwitterionic EYPC/cholesterol (10 : 1, w/w) liposomes compared to negatively charged EYPE/EYPG (7 : 3, w/w) liposomes. The blue shift of the fluorescence emission maximum of ME-D in zwitterionic EYPC/cholesterol (10 : 1, w/w) liposomes was much smaller than in negatively charged EYPE/EYPG (7 : 3, w/w) liposomes. These results suggested that the improvement in therapeutic index/cell selectivity of ME-D is correlated with its less permeability to zwitterionic membranes.

Mechanism and Regulation of Amino Acid Transport in Mammary Gland - Review -

  • Kansal, Vinod K.;Sharma, Rekha
    • Asian-Australasian Journal of Animal Sciences
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    • 제14권5호
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    • pp.710-719
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    • 2001
  • Several amino acid transport systems in mammary gland have been characterized during the last few years. These systems may be divided into two broad categories based on whether they are sodium-dependent or $Na^{+}$-independent, and each of these categories is subdivided into 3 groups depending on whether the systems prefer zwitterionic, cationic or anionic substrates. The zwitterion preferring transport processes in mammary gland are $Na^{+}$-dependent system A and $Na^{+}$-independent systems L and T. System $y^{+}$ is a $Na^{+}$-independent transporter of cationic amino acids and $X_{AG^{-}}$ is a $Na^{+}$-dependent system for anionic amino acids. A ($Na^{+}+Cl^{-}$)-dependent system, selective for $\beta$-amino acids has been reported in rat mammary tissue. In addition, there is yet another class of transporters that have still broader specificity. The $Na^{+}$-dependent systems $BCl^{-}$-dependent and $BCl^{-}$-independent and $Na^{+}$-independent system $y^{+}L$ have been reported to mediate the transport of zwitterionic as well as cationic amino acids. Each system has been characterized with respect to its substrate specificity, affinity, kinetics and ion-dependence. Transport of amino acids by mammary tissue is regulated by i) the intracellular substrate concentration, ii) lactogenic hormones and iii) milk stasis. Four of the above transport systems (i.e. A, L, $y^{+}$ and $BCl^{-}$-independent) are up-regulated by lactogenic hormones (insulin, cortisol and prolactin) in mammary gland.

The crystal and molecular structure of $\gamma$-hydroxy-.$\beta$-amino butyric acid

  • Kim, Yang-Bae
    • Archives of Pharmacal Research
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    • 제8권1호
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    • pp.1-6
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    • 1985
  • The crystal structure or $\gamma$-hydroxy-$\betha$-aminobutyric acid was determined by MULTAN system with X-ray intensity data on a diffractometer and refined by the least-squares method to an R-value 0.034 for 711 reflections. The crystals were orthorhombic, space group $P2_{1}2_{1}2_{1}$, Z = 4, with a = 10.220, b = 8.257 and c = 6.556$\AA$. The molecule takes the zwitterionic form and skeletal conformation is trans-transform. The molecules are held together by intra-and intermolecular NH-O and OH--O hydrogen bonds.

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4-아미노피리딘 – HCl, –HBr 복합체에 대한 양자화학적 연구 : 즈비터이온의 안정성 (Stability of the Zwitterionic form of 4-aminopyrimidine HCl and -HBr Complexes: Computational Study)

  • 황태규;박성우;윤영삼;이성렬
    • 대한화학회지
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    • 제53권2호
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    • pp.133-136
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    • 2009
  • 4-아미노피리딘 (4AP)–HCl와 –HBr 복합체에 대한 양자화학적 계산을 수행하였다. 전하분리된 (즈비 터이온) 형태의 [4AP$H^+-Cl^-$]는 안정하지 않으나, [4AP$H^+-Br^-$]은 안정하여 저온기체상에서 관찰될 것으로 예측되었다. 이것은 HCl에 비하여 HBr의 해리에너지가 작다는 사실과, 4AP의 아미노기가 HBr의 “용매”로 작용 한 결과로 해석되었다.

Tandem Mass Spectrometric Evidence for the Involvement of a Lysine Basic Side Chain in the Coordination of Zn(II) Ion within a Zinc-bound Lysine Ternary Complex

  • Yu, Sung-Hyun;Lee, Sun-Young;Chung, Gyu-Sung;Oh, Han-Bin
    • Bulletin of the Korean Chemical Society
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    • 제25권10호
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    • pp.1477-1483
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    • 2004
  • We present the tandem mass spectrometry applications carried out to elucidate the coordination structure of Zn(II) bound lysine ternary complexes, $(Zn+Lys+Lys-H)^+$, which is a good model system to represent a simple (metallo)enzyme-substrate complex (ES). In particular, experimental efforts were focused on revealing the involvement of a lysine side chain ${\varepsilon}$-amino group in the coordination of $Zn^{2+}$ divalent ions. MS/MS fragmentation pattern showed that all the oxygen species within a complex fell off in the form of $H_2O$ in contrast to those of other ternary complexes containing amino acids with simple side chains (4-coordinate geometries, Figure 1a), suggesting that the lysine complexes have different coordination structures from the others. The participation of a lysine basic side chain in the coordination of Zn(II) was experimentally evidenced in MS/MS for $N{\varepsilon}$-Acetyl-L-Lys Zn(II) complexes with acetyl protection groups as well as in MS/MS for the ternary complexes with one $NH_3$ loss, $(Zn+Lys+Lys-NH_3-H)^+$. Detailed structures were predicted using ab initio calculations on $(Zn+Lys+Lys-H)^+$ isomers with 4-, 5-, and 6-coordinate structures. A zwitterionic 4-coordinate complex (Figure 7d) and a 5-coordinate structure with distorted bipyramidal geometry (Figure 7b) are found to be most plausible in terms of energy stability and compatibility with the experimental observations, respectively.