Chemistry Reference
In-Depth Information
X
8
X
7
X
7
X
8
X
8
X
5
X
6
X
7
X
6
X
5
(1) Piperidine, DMF
(2) FmocAAOH, BOP, HOBT
(3) Repeat (1) and (2) 10 ti
mes
X
7
X
8
X
4
X
3
FmocHN
X
2
X
1
(4) (1), then Ac
2
O, py
(5) CF
3
CO
2
H, then HPLC
X
8
X
3
X
4
X
7
160 mg of rink
amide resin
0.25 mmol/g
X
6
X
5
X
7
X
8
X
5
X
6
X
7
X
8
X
7
X
8
O
NH
OH
N
O
NH
O
N
HN
O
N
N
O
O
HN
HN
NH
N
N
OH
HN
O
HN
HO
O
O
HN
O
H
N
NH
O
O
N
NH
H
H
O
O
NH
NH
N
H
O
O
O
HN
N
HO
HN
HN
NH
N
H
O
O
O
HN
H
2
N
NH
O
O
H
2
N
N
O
NH
2
H
N
H
O
O
O
HN
HN
N
O
O
NH
N
O
HN
HN
O
N
NH
HO
O
NH
O
H
N
NH
O
HO
NH
O
N
H
HN
O
N
HN
N
O
HN
H
N
H
O
O
NH
O
O
O
N
O
N
H
OH
O
N
HN
N
NH
H
OH
O
N
H
O
NH
C11
(19.7 mg, 8% isolated yield)
FIGURE 15.1
Synthesis and structure of the third-generation peptide dendrimer
C11
(AcHisSer)
8
(DapHisLeu)
4
(DapLysVal)
2
DapIleValNH
2
(Dap
ΒΌ
branching
L
-2,3-diaminopro-
panoic acid) identified by screening as an esterase dendrimer [14].
the branches, and at the branches' ends (Figure 15.1). These peptide dendrimers are
identical to proteins in terms of composition and only differ in their topology.
Furthermore, they can be optimized iteratively by amino acid substitutions in a
manner similar to the natural evolution of proteins. We present our progress toward
protein-like functions in the area of artificial enzymes, metal binding, and glyco-
peptide dendrimers, as well as structural studies by spectroscopic and molecular
modeling methods.
