Adsorption of amino acids by fullerenes and fullerene nanowhiskers. Issue 6 (27th November 2015)
- Record Type:
- Journal Article
- Title:
- Adsorption of amino acids by fullerenes and fullerene nanowhiskers. Issue 6 (27th November 2015)
- Main Title:
- Adsorption of amino acids by fullerenes and fullerene nanowhiskers
- Authors:
- Hashizume, Hideo
Hirata, Chika
Fujii, Kazuko
Miyazawa, Kun'ichi - Abstract:
- Abstract: We have investigated the adsorption of some amino acids and an oligopeptide by fullerene (C60 ) and fullerene nanowhiskers (FNWs). C60 and FNWs hardly adsorbed amino acids. Most of the amino acids used have a hydrophobic side chain. Ala and Val, with an alkyl chain, were not adsorbed by the C60 or FNWs. Trp, Phe and Pro, with a cyclic structure, were not adsorbed by them either. The aromatic group of C60 did not interact with the side chain. The carboxyl or amino group, with the frame structure of an amino acid, has a positive or negative charge in solution. It is likely that the C60 and FNWs would not prefer the charged carboxyl or amino group. Tri-Ala was adsorbed slightly by the C60 and FNWs. The carboxyl or amino group is not close to the center of the methyl group of Tri-Ala. One of the methyl groups in Tri-Ala would interact with the aromatic structure of the C60 and FNWs. We compared our results with the theoretical interaction of 20 bio-amino acids with C60 . The theoretical simulations showed the bonding distance between C60 and an amino acid and the dissociation energy. The dissociation energy was shown to increase in the order, Val < Phe < Pro < Asp < Ala < Trp < Tyr < Arg < Leu. However, the simulation was not consistent with our experimental results. The adsorption of albumin (a protein) by C60 showed the effect on the side chains of Try and Trp. The structure of albumin was changed a little by C60 . In our study Try and Tyr were hardly adsorbed by C60Abstract: We have investigated the adsorption of some amino acids and an oligopeptide by fullerene (C60 ) and fullerene nanowhiskers (FNWs). C60 and FNWs hardly adsorbed amino acids. Most of the amino acids used have a hydrophobic side chain. Ala and Val, with an alkyl chain, were not adsorbed by the C60 or FNWs. Trp, Phe and Pro, with a cyclic structure, were not adsorbed by them either. The aromatic group of C60 did not interact with the side chain. The carboxyl or amino group, with the frame structure of an amino acid, has a positive or negative charge in solution. It is likely that the C60 and FNWs would not prefer the charged carboxyl or amino group. Tri-Ala was adsorbed slightly by the C60 and FNWs. The carboxyl or amino group is not close to the center of the methyl group of Tri-Ala. One of the methyl groups in Tri-Ala would interact with the aromatic structure of the C60 and FNWs. We compared our results with the theoretical interaction of 20 bio-amino acids with C60 . The theoretical simulations showed the bonding distance between C60 and an amino acid and the dissociation energy. The dissociation energy was shown to increase in the order, Val < Phe < Pro < Asp < Ala < Trp < Tyr < Arg < Leu. However, the simulation was not consistent with our experimental results. The adsorption of albumin (a protein) by C60 showed the effect on the side chains of Try and Trp. The structure of albumin was changed a little by C60 . In our study Try and Tyr were hardly adsorbed by C60 and FNWs. These amino acids did not show a different adsorption behavior compared with other amino acids. The adsorptive behavior of mono-amino acids might be different from that of polypeptides. … (more)
- Is Part Of:
- Science and technology of advanced materials. Volume 16:Issue 6(2015)
- Journal:
- Science and technology of advanced materials
- Issue:
- Volume 16:Issue 6(2015)
- Issue Display:
- Volume 16, Issue 6 (2015)
- Year:
- 2015
- Volume:
- 16
- Issue:
- 6
- Issue Sort Value:
- 2015-0016-0006-0000
- Page Start:
- Page End:
- Publication Date:
- 2015-11-27
- Subjects:
- adsorption -- amino acid -- fullerene -- fullerene nanowhisker
Materials -- Technological innovations -- Periodicals
620.112 - Journal URLs:
- http://iopscience.iop.org/1468-6996 ↗
https://tandfonline.com/toc/tsta20/current ↗
http://ioppublishing.org/ ↗ - DOI:
- 10.1088/1468-6996/16/6/065005 ↗
- Languages:
- English
- ISSNs:
- 1468-6996
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8134.254650
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 8468.xml