LL-37 KR-12

General Information


DRACP ID  DRACP00648

Peptide Name   LL-37 KR-12

Sequence  KRIVQRIKDFLR

Sequence Length  12

UniProt ID  Not available

PubChem CID  Not available

Origin  Synthetic

Type  Synthetic peptide

Classification

  

Active ACP



Activity Information


Cell Line Disease Cancer Classified Activity Assay Testing Time Literature
CaCo-2 Colon adenocarcinoma Carcinoma EC50=125µg/ml MTT assay 24h 1
A431 Skin squamous cell carcinoma Carcinoma EC50=31.2µg/ml MTT assay 24h 1

Hemolytic Activity  Human erythrocytes: 50% Hemolysis>800µM; 10.6% Hemolysis=100µM; <5% Hemolysis=256µg/ml; Rabbit erythrocytes: 73% Hemolysis=125µg/ml

Normal (non-cancerous) Cytotoxicity  NIH 3T3: EC50=0.8µg/ml; HaCat: IC50=74.6µg/ml

Target  Not available

Affinity  Not available

Mechanism  Not available

Nature  Anticancer; Antibacterial



Structure Information


PDB ID  Not available

Predicted Structure  DRACP00648

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  C71H126N24O16

Absent amino acids  ACEGHMNPSTWY

Common amino acids  R

Mass  176832

Pl  12.24

Basic residues  5

Acidic residues  1

Hydrophobic residues  5

Net charge  4

Boman Index  -4834

Hydrophobicity  -70.83

Aliphatic Index  121.67

Half Life 
  Mammalian: 1.1 hour
  Yeast: 3 min
  E.coli: 2 min

Extinction Coefficient cystines  0

Absorbance 280nm  0

Polar residues  0

Amino acid distribution



Literature Information


Literature 1

Pubmed ID 27907988

Title  KR12 peptide associated with cyclodextrin: Antimicrobial and antitumor activities

Doi 10.1116/1.4968880

Year  2016

Literature 2

Pubmed ID 24105706

Title  Short KR-12 analogs designed from human cathelicidin LL-37 possessing both antimicrobial and antiendotoxic activities without mammalian cell toxicity

Doi 10.1002/psc.2552

Year  2013

Literature 3

Pubmed ID 24307932

Title  Structural location determines functional roles of the basic amino acids of KR-12, the smallest antimicrobial peptide from human cathelicidin LL-37

Doi 10.1039/C3RA42599A

Year  2013

Literature 4

Pubmed ID 32019109

Title  Lipidated Analogs of the LL-37-Derived Peptide Fragment KR12-Structural Analysis, Surface-Active Properties and Antimicrobial Activity

Doi 10.3390/ijms21030887

Year  2020

Patent

Patent ID Not available

Patent Title  Not available

Other Iinformation  Not available

Other Published ID  Not available




DRACP is developed by Dr.Zheng's team.