Difference between revisions of "Team:XJTLU-CHINA/PeptideProduction"

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        <div class="para">
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            <h1>Anti-Microbial Peptide</h1>
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            <p style="font-size:20px">
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                Anti-microbial peptide (AMP) is a part of the innate immune system of most multi-cellular organisms to counter microbial
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                infections (Margitta and Torsten, 1999). The cationic and amphipathic α-helix structure is the most wildly
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                conformation in those peptides but some hydrophobic α-helical peptides which possess antimicrobial activity.
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                This year we choose three different cationic antimicrobial peptides which encompass α-helical conformation
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                in our project.
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            </p>
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            <p style="font-size:20px">
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                Figure 1 shows the molecular mechanism of cationic AMPs α-helical structure. Most of cationic AMPs associate with lipid group
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                of bacteria membrane. The α-helical structure disrupt the packing of lipid molecules such that the membrane
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                becomes leaky (Rocca et al., 1999).
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            </p>
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        <div class="fig" align="center">
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                <img width="650px" src="https://static.igem.org/mediawiki/2017/9/99/Peptide_Production_1.png">
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                <figcaption>Figure 1: The interaction mechanism of cationic α-helical structure of Anti-microbial peptides. The α-helical
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                    structure insert into the bacteria Lipid bilayer in aqueous solution. Following insertion of the peptide,
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                    the bilayer membrane permeability may be varied.</figcaption>
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            </figure>
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        <div class="para">
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            <h1>LL-37</h1>
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            <p style="font-size:20px">
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                LL-37 is the only cathelicidin-derived antimicrobial peptide found in humans (Dürr, Sudheendra and Ramamoorthy, 2006). Mature
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                LL-37 has 37 amino acid residues starting with two leucines (NH2-LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES-COOH).
 +
                The peptide is cleaved from a larger protein, hCAP-18 by extracellular proteolysis of proteinase 3 from the
 +
                C-terminal end of hCAP18 (Patricia, 2010; Ramos, Domingues, and Gama, 2011). The peptide composed of two
 +
                mainly parts: from residue Leu2 to Leu31 is α-helical structure (Fig 2b) and 6 residues form loop structure
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                (Fig 2a).
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            </p>
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            <p style="font-size:20px">
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                Ramos, Domingues, and Gama (2011) also reported that LL-37 has additional roles such as regulating the inflammatory response
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                to wound or infection sites, binding and neutralizing LPS, and wound closure apart from anti-microbial property
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                (Figure 2c).
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                <img width="650px" src="https://static.igem.org/mediawiki/2017/d/de/Peptide_Production_2a.png">
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                <figcaption>Figure 2a: LL-37 structure and residues（PDB 2K6O）</figcaption>
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            </figure>
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            <figure>
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                <img width="650px" src="https://static.igem.org/mediawiki/2017/2/29/Peptide_Production_2b.png">
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                <figcaption>Figure 2b: LL-37 secondary structure prediction (predicted by http://www.compbio.dundee.ac.uk/jpred/index.html
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                    ).
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                </figcaption>
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            <figure>
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                    <img width="650px" src="https://static.igem.org/mediawiki/2017/3/3b/Peptide_Production_2c.png">
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                    <figcaption>Figure 2c: Biological functions of LL-37 (Ramos, Domingues, and Gama, 2011)</figcaption>
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                </figure>
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Revision as of 08:57, 30 October 2017

Peptide Production

Peptide Production

Anti-Microbial Peptide

Anti-microbial peptide (AMP) is a part of the innate immune system of most multi-cellular organisms to counter microbial infections (Margitta and Torsten, 1999). The cationic and amphipathic α-helix structure is the most wildly conformation in those peptides but some hydrophobic α-helical peptides which possess antimicrobial activity. This year we choose three different cationic antimicrobial peptides which encompass α-helical conformation in our project.

Figure 1 shows the molecular mechanism of cationic AMPs α-helical structure. Most of cationic AMPs associate with lipid group of bacteria membrane. The α-helical structure disrupt the packing of lipid molecules such that the membrane becomes leaky (Rocca et al., 1999).

Figure 1: The interaction mechanism of cationic α-helical structure of Anti-microbial peptides. The α-helical structure insert into the bacteria Lipid bilayer in aqueous solution. Following insertion of the peptide, the bilayer membrane permeability may be varied.

LL-37

LL-37 is the only cathelicidin-derived antimicrobial peptide found in humans (Dürr, Sudheendra and Ramamoorthy, 2006). Mature LL-37 has 37 amino acid residues starting with two leucines (NH2-LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES-COOH). The peptide is cleaved from a larger protein, hCAP-18 by extracellular proteolysis of proteinase 3 from the C-terminal end of hCAP18 (Patricia, 2010; Ramos, Domingues, and Gama, 2011). The peptide composed of two mainly parts: from residue Leu2 to Leu31 is α-helical structure (Fig 2b) and 6 residues form loop structure (Fig 2a).

Ramos, Domingues, and Gama (2011) also reported that LL-37 has additional roles such as regulating the inflammatory response to wound or infection sites, binding and neutralizing LPS, and wound closure apart from anti-microbial property (Figure 2c).

Figure 2a: LL-37 structure and residues（PDB 2K6O）
Figure 2b: LL-37 secondary structure prediction (predicted by http://www.compbio.dundee.ac.uk/jpred/index.html ).
Figure 2c: Biological functions of LL-37 (Ramos, Domingues, and Gama, 2011)