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Exact(7)
We note that the modified peptide was eluted after the un-modified peptide (see peak 7 & 8 in Fig. S5C), demonstrating that the former was more hydrophobic than the latter.
Besides obtaining sequence information of the two peptides with un-acetylated and acetylated lysine 20 (data not shown), we also noticed that the modified peptide was eluted about 4 minutes after the un-modified one (Fig. 4C & 4D), which is in agreement with the notion of acetylation increasing the hydrophobicity of a molecule [37].
The modified peptide was presented in liposome to immunize rabbits.
As might be expected, the modified peptide was able to target membrane surface with a moderate antibacterial potency (MIC = 50 100 μg/ml).
Mass spectrometry analysis was used to corroborate the identity of the protein by peptide mass fingerprinting; also, the modified peptide was fragmented and sequenced by mass spectrometry, corroborating thus the inserted residues.
The purity of the modified hydrazine modified peptide was >95% as determined by C18 reverse phase HPLC.
Similar(53)
The modified peptide is cyclized through an amide linkage between the cysteine and lysine residues and thus is more stable.
The binding affinity and receptor selectivity of the modified peptide were controlled using the corresponding isolated immobilised integrins.
The antimicrobial activity of all the modified peptides was also determined so that peptides with both optimal stability and activity could be identified.
D1D2 binding to modified peptides was comparable for human and mouse.
Identity of the modified peptides was verified by MS/MS sequencing.
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