Anticancer peptide NK-2 targets cell surface sulphated glycans rather than sialic acids

Biological Chemistry

Volumn 393, Issue 8, 2012, Pages 817-827

  Gross, Stephanie ^a   Andrä, Jörg ^a,b  

^a RESEARCH CENTER BORSTEL   (Germany)

^b HAMBURG UNIVERSITY OF APPLIED SCIENCES   (Germany)

Author keywords

Antimicrobial peptide; Cathelicidin; Glycan array; Glycocalyx; Melittin; NK lysin

Indexed keywords

ANTIMICROBIAL PEPTIDE LL 32; ANTINEOPLASTIC AGENT; CHONDROITIN SULFATE; FETUIN; GLYCAN DERIVATIVE; MELITTIN; PEPTIDE NK 2; POLYPEPTIDE ANTIBIOTIC AGENT; SIALIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

ALPHA HELIX; CANCER CELL; CELL MEMBRANE; CELL METABOLISM; CELL PERMEABILIZATION; CELL SURFACE; COMPETITIVE INHIBITION; CONTROLLED STUDY; CYTOTOXICITY; ENTHALPY; ENZYME MODIFICATION; HUMAN; HUMAN CELL; MALE; MICROARRAY ANALYSIS; PRIORITY JOURNAL; PROSTATE CANCER; REVIEW; TARGET CELL;

AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; ANTINEOPLASTIC AGENTS; CARBOHYDRATE SEQUENCE; CELL LINE, TUMOR; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELL SURVIVAL; HUMANS; MALE; MELITTEN; MOLECULAR SEQUENCE DATA; PEPTIDES; POLYSACCHARIDES; PROSTATIC NEOPLASMS; SIALIC ACIDS; SULFATES;

EID: 84867815230     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2012-0136     Document Type: Review

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