Peptide name : Lunasin

Source/Organism : Lima bean

Linear/Cyclic : Not found

Chirality : L

Peptide length: 20

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Colorectal cancer

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 2178.4251 Dalton

Aliphatic index : 0.295

Instability index : -5.545

Hydrophobicity (GRAVY) : -0.34

Isoelectric point : 6.0489

Charge (pH 7) : -0.2667

Aromaticity : 0.1

Molar extinction coefficient (cysteine, cystine): (0, 125)

Hydrophobic/hydrophilic ratio : 1

hydrophobic moment : -1.147

Missing amino acid : W,H,Q,M,I,Y,V

Most occurring amino acid : T

Most occurring amino acid frequency : 3

Least occurring amino acid : K

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.3, 0.3)

SMILES Notation: CC(C)C[C@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CS)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)O)[C@@H](C)O)[C@@H](C)O

1 : Wong JH and Ng TB. Lunatusin, a trypsin-stable antimicrobial peptide from lima beans (Phaseolus lunatus L.). Peptides. 2005; 26:2086-92. doi: 10.1016/j.peptides.2005.03.004

2 : Wang G, et al. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009; 37:D933-7. doi: 10.1093/nar/gkn823

Paper title : Lunatusin, a trypsin-stable antimicrobial peptide from lima beans (Phaseolus lunatus L.).

Doi : https://doi.org/10.1016/j.peptides.2005.03.004

Abstract : An anti-fungal peptide designated as lunatusin, with a molecular mass around 7kDa, was purified from the seeds of Chinese lima bean (Phaseolus lunatus L.). The peptide was isolated using a simple protocol consisting of affinity chromatography on Affi-gel blue gel and gel filtration on Superdex 75. Lunatusin exerted an anti-fungal activity toward fungal species such as Fusarium oxysporum, Mycosphaerella arachidicola and Botrytis cinerea, and an antibacterial action on, Bacillus megaterium, Bacillus subtilis, Proteus vulgaris and Mycobacterium phlei. It also inhibited proliferation in the breast cancer cell line MCF-7. Lunatusin reduced the activity of HIV-1 reverse transcriptase and it also inhibited translation in a cell-free rabbit reticulocyte lysate system. Its anti-fungal activity was retained after incubation with trypsin. Lunatusin elicited a mitogenic response from mouse splenocytes.

Paper title : APD2: the updated antimicrobial peptide database and its application in peptide design.

Doi : https://doi.org/10.1093/nar/gkn823

Abstract : The antimicrobial peptide database (APD, http://aps.unmc.edu/AP/main.php) has been updated and expanded. It now hosts 1228 entries with 65 anticancer, 76 antiviral (53 anti-HIV), 327 antifungal and 944 antibacterial peptides. The second version of our database (APD2) allows users to search peptide families (e.g. bacteriocins, cyclotides, or defensins), peptide sources (e.g. fish, frogs or chicken), post-translationally modified peptides (e.g. amidation, oxidation, lipidation, glycosylation or d-amino acids), and peptide binding targets (e.g. membranes, proteins, DNA/RNA, LPS or sugars). Statistical analyses reveal that the frequently used amino acid residues (>10%) are Ala and Gly in bacterial peptides, Cys and Gly in plant peptides, Ala, Gly and Lys in insect peptides, and Leu, Ala, Gly and Lys in amphibian peptides. Using frequently occurring residues, we demonstrate database-aided peptide design in different ways. Among the three peptides designed, GLK-19 showed a higher activity against Escherichia coli than human LL-37.