Chemistry Reference
In-Depth Information
2.6 Conclusions and Outlook
We have shown a short overview on the amazing amount of work that has been done in
the past 15 years within the newborn but very promising field of foldamers. Many new
monomers have been prepared and introduced into oligomers. They may have an aliphatic
or an aromatic skeleton, may mimic a-, b-, g-ord-amino acids or even not resemble an
amino acid at all, but they all have the common characteristic of promoting a folded struc-
ture. At the moment several groups are engaged in the study of foldamers able to promote
the formation of secondary, tertiary and even quaternary structures, as we previously
briefly reported. These supramolecular structures may have noteworthy applications as
readily tunable molecular frameworks for the recognition and inhibition of bacterial cell
membranes, protein-RNA interactions, protein-protein interactions and enzymes.
Metallofoldamers have a central role in this study, as they may efficiently mimic metal-
loproteins. They have an impressive ability to form single-handed helical structures and
other chiral architectures. Moreover, they may be applied as sensors due to their selective
folding when binding to a specific metal ion or as responsive materials.
While several overviews, reviews and even books have been published in recent years
in the field of foldamers, a systematic presentation of metallofoldamers has never been
published till now. This topic fills the gap and is an important milestone in the study of
the design, preparation and application of metallofoldamers.
References
1. Gellman, S.H. (1998) Foldamers: a manifesto.
Acc. Chem. Res.
,
31
, 173-180.
2. Nielsen, P.E., Egholm, M., Berg, R.H., and Buchardt, O. (1991) Sequence-selective
recognition of DNA by strand displacement with a thymine-substituted polyamide.
Science
,
254
, 1497-1500.
3. Simon, R.J., Kania, R.S., Zuckermann, R.N.
et al.
(1992). Peptoids: a modular approach to
drug discovery.
Proc. Natl Acad. Sci. USA
,
89
, 9367-9371.
4. Hill, D.J., Mio, M.J., Prince, R.B.
et al.
(2001) A field guide to foldamers.
Chem. Rev.
,
101
,
3893-4011.
5. Hecht, S. and Huc, I. (2007)
Foldamers: Structure, Properties, and Applications
, Wiley-VCH,
Weinheim.
6. (a) Cubberley, M.S. and Iverson, B.L. (2001) Models of higher-order structure: foldamers and
beyond.
Curr. Opin. Chem. Biol.
,
5
, 650-653; (b) Seebach, D., Beck, A.K., and Bierbaum, D.
J. (2004) The world of (- and (-peptides comprised of homologated proteinogenic amino acids
and other components.
Chem. Biodivers.
,
1
, 1111-1239; (c) Sanford, A.R., Yamato, K., Yang,
X.
et al.
(2004) Well-defined secondary structures.
Eur. J. Biochem.
,
271
, 1416-1425;
(d) Cheng, R.P. (2004) Beyond
de novo
protein design -
de novo
design of non-natural folded
oligomers.
Curr. Opin. Struct. Biol.
,
14
, 512-520; (e) Balbo Block, M.A., Kaiser, C., Khan,
A., and Hecht, S. (2005) Discrete organic nanotubes based on a combination of covalent and
non-covalent approaches.
Top. Curr. Chem.
,
245
, 89-150; (f) Fulop, F., Martinek, T.A., and
Toth, G.K. (2006) Application of alicyclic b-amino acids in peptide chemistry.
Chem. Soc.
Rev.
,
35
, 323-334. (g) Goodman, C.M., Choi, S., Shandler, S., and DeGrado, W.F. (2007)
Foldamers as versatile frameworks for the design and evolution of function.
Nat. Chem. Biol.
,
3
, 252-262; (h) Bautista, A.D., Craig, C.J., Harker, E.A., and Schepartz, A. (2007) Sophistica-
tion of foldamer form and function
in vitro
and
in vivo
.
Curr. Opin. Chem. Biol.
,
11
, 685-692;
Search WWH ::
Custom Search