LL-37 (15-32)[E1G], GF-17

General Information


DRACP ID  DRACP03512

Peptide Name   LL-37 (15-32)[E1G], GF-17

Sequence  GFKRIVQRIKDFLRNLV

Sequence Length  17

UniProt ID  P49913 

PubChem CID  Not available

Origin  Synthetic

Type  Synthetic peptide

Classification

  

Active ACP



Activity Information


Hemolytic Activity  Not available

Normal (non-cancerous) Cytotoxicity  Not available

Target  Not available

Affinity  Not available

Mechanism  Not available

Nature  Anticancer; Antibacterial; Antiviral



Structure Information


PDB ID  2L5M 

Predicted Structure  DRACP03512

Helicity  Not available

Linear/Cyclic  Linear

Disulfide/Other Bond  Not available

N-terminal Modification  Free

C-terminal Modification  Amidation

Other Modification  None

Chiral  L



Physicochemical Information


Formula  C97H164N30O22

Absent amino acids  ACEHMPSTWY

Common amino acids  R

Mass  238813

Pl  12.24

Basic residues  5

Acidic residues  1

Hydrophobic residues  8

Net charge  4

Boman Index  -4210

Hydrophobicity  -9.41

Aliphatic Index  125.88

Half Life 
  Mammalian: 2.8 hour
  Yeast: 10 min
  E.coli: 2 min

Extinction Coefficient cystines  0

Absorbance 280nm  0

Polar residues  2

Amino acid distribution



Literature Information


Literature 1

Pubmed ID 34959645

Title  Structure and Activity of a Selective Antibiofilm Peptide SK-24 Derived from the NMR Structure of Human Cathelicidin LL-37

Doi Not available

Year  2021

Literature 2

Pubmed ID 32252021

Title  Engineered Human Cathelicidin Antimicrobial Peptides Inhibit Ebola Virus Infection

Doi Not available

Year  2021

Literature 3

Pubmed ID 30800727

Title  Amino Acid Composition Determines Peptide Activity Spectrum and Hot-Spot-Based Design of Merecidin

Doi Not available

Year  2018

Literature 4

Pubmed ID 19581460

Title  Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37

Doi Not available

Year  2009

Literature 5

Pubmed ID 28450045

Title  Arginine-lysine positional swap of the LL-37 peptides reveals evolutional advantages of the native sequence and leads to bacterial probes

Doi Not available

Year  2017

Literature 6

Pubmed ID 22083479

Title  Decoding the functional roles of cationic side chains of the major antimicrobial region of human cathelicidin LL-37

Doi Not available

Year  2012

Literature 7

Pubmed ID 20086159

Title  Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database

Doi N

Year 

Patent

Patent ID Not available

Patent Title  Not available

Other Iinformation  Not available

Other Published ID  Not available




DBAASP ID  6070

DRACP is developed by Dr.Zheng's team.