Table 6. AAA of AMP (Sequence: GIGKFLKKAKKFAKAFVKILKK-Ahx-C; MW: 2706.6 Da) Grafted or Adsorbed onto NPa.
| nmol
(hydrolyzed conjugated) |
experimental
ratio |
|||||
|---|---|---|---|---|---|---|
| amino acid | AMP-NP immobilized | AMP-NP adsorbed | theoretical ratio | AMP-NP immobilized | AMP-NP adsorbed | |
| glycinec | G | 75.7 | 12.3 | 2 | 2 | 3 |
| alanine | A | 86.5 | 15.2 | 3 | 2 | 4 |
| valinecd | V | 31.2 | 3.7 | 1 | 1 | 1 |
| isoleucinec | I | 68.4 | 10.7 | 2 | 2 | 3 |
| leucinec | L | 64.9 | 8.6 | 2 | 2 | 2 |
| phenylalaninecd | F | 115.5 | 10.9 | 3 | 3 | 3 |
| lysined | K | 237.1 | 33.2 | 9 | 7 | 9 |
| AMP contentb | 35.6 | 3.7 | ||||
| AMP mass (μg AMP/1011 NP) | 96 | 9.9 | ||||
The AMP content was calculated by the average through the ratios of each hydrolyzed AA (nmol) considered for the calculation and the respective experimental ratio. The AMP mass corresponds to the final AMP-content (μmol) x MWAMP (Da).
nmols/residue, estimated.
Amino acids are considered for the calculation of immobilized.
Amino acids are considered for the calculation of the adsorbed peptide quantity.