Table 1 Amino acid sequences, molecular weights, charge, and hydrophobicity values of the mutations of the parent peptides chensinin-1.

From: Antimicrobial and anti-inflammatory activities of three chensinin-1 peptides containing mutation of glycine and histidine residues

Peptides

Amino acid sequences

Net charge

H a

Mass calc./obs b

Chensinin-1

SAVGRHGRRFGLRKHRKH

7

4.2889

2155.5/2155.8

MC1-1

SAVWRHWRRFWLRKHRKH

7

9.6888

2542.9/2542.8

MC1-2

SAVWRWRRFWLRKRK

7

11.626

2131.5/2131.2

MC1-3

SAVWRRWRRFWLRKRRKR

10

9.788

2600.1/2600

  1. aThe mean hydrophobicities (H) of the peptides calculated using the hydrophobicity scales were the total hydrophobicity (sum of all residue hydrophobicity indices) divided by the number of residues.
  2. bMass calc./obs. represented calculated molecular masses based on the amino acid sequence determined by Edman degradation and observed molecular masses determined by Maldi-TOF MS.
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