Cyclic azapeptides with angiogenic effect

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

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C514S017400, C530S317000, C530S329000, C530S330000

Reexamination Certificate

active

06534478

ABSTRACT:

SUMMARY OF THE INVENTION
The invention relates to compounds of the formula I
cyclo-(aArg-aGly-aAsp-aX-aY)  I
in which
aArg is Arg or aza-Arg,
aGly is Gly or aza-Gly,
aAsp is Asp or aza-Asp,
aX, aY in each case independently of one another are an amino acid residue selected from a group consisting of Ala, Asn, Asp, Arg, Cys, Gln, Glu, Gly, His, Ile, Leu, Lys, Met, Nle, Orn, Phe, Phg, Pro, Ser, Thr, Tic, Trp, Tyr, Val, NH—Q—CO—
or
the corresponding aza-amino acids,
Q is alkylene having 1-6 C atoms,
where
in at least one of the amino acids mentioned in formula I the C
&agr;
carbon is replaced by nitrogen,
the amino acids mentioned can also be derivatized, and the amino acid residues are linked to one another in peptide fashion via the a-amino or aza group and &agr;-carboxyl groups,
and if there are radicals of optically active amino acids and amino acid derivatives, both the D and the L forms are included,
and their salts.
Similar compounds of cyclic peptides are disclosed, for example, in EP 0 632 053, DE 195 38 741 or EP 0 683 173.
DETAILED DESCRIPTION OF THE INVENTION
The invention is based on the object of finding novel compounds having valuable properties, in particular those which can be used for the production of medicaments.
It has been found that the compounds of the formula I and their salts have very valuable pharmacological properties combined with good tolerability. They act especially as integrin inhibitors, in particular inhibiting the interactions of the &agr;
v
-, &bgr;
3
- or &bgr;
5
-integrin receptors with ligands, such as, for example, the binding of fibrinogen to the &bgr;
3
-integrin receptor. The compounds show particular activity in the case of the integrins &agr;
v
&bgr;
1
, &agr;
v
&bgr;
3
, &agr;
v
&bgr;
5
, &agr;
IIb
&bgr;
3
and also &agr;
v
&bgr;
6
and &agr;
v
&bgr;
8
, in particular potent selective inhibitors of the vitronectin receptor &agr;
v
&bgr;
3
have been found.
This action can be demonstrated, for example, by the method which is described by J. W. Smith et al. in J. Biol. Chem. 265, 12267-12271 (1990). The dependence of the origin of angiogenesis on the interaction between vascular integrins and extracellular matrix proteins is described by P. C. Brooks, R. A. Clark and D. A. Cheresh in Science 264, 569-71 (1994).
The possibility of the inhibition of this interaction and thus for the initiation of apoptosis (programmed cell death) of angiogenic vascular cells by a cyclic peptide is described by P. C. Brooks, A. M. Montgomery, M. Rosenfeld, R. A. Reisfeld, T.-Hu, G. Klier and D. A. Cheresh in Cell 79, 1157-64 (1994).
Compounds of the formula I, which block the interaction of integrin receptors and ligands, such as, for example, of fibrinogen on the fibrinogen receptor (glycoprotein IIb/IIIa), prevent, as GPIIb/IIIa antagonists, the spread of tumour cells by metastasis. This is confirmed by the following observations:
The compounds can inhibit the binding of metalloproteinases to integrins and thus prevent the cells being able to utilize the enzymatic activity of the proteinase. An example is to be found in the inhibitability of the binding of MMP-2 (matrix metalloproteinase-2) to the vitronectin receptor &agr;
v
&bgr;
3
by a cyclo-RGD peptide, as described in P. C. Brooks et al., Cell 85, 683-693 (1996).
The spread of tumour cells from a local tumour into the vascular system takes place through the formation of microaggregates (microthrombi) by interaction of the tumour cells with blood platelets. The tumour cells are screened by protection in the microaggregate and are not recognized by the cells of the immune system. The microaggregates can fix to vascular walls, by means of which a further penetration of tumour cells into the tissue is facilitated. Since the formation of the microthrombi is mediated by fibrinogen formation on the fibrinogen receptors on activated blood platelets, the GPIIa/IIIb antagonists can be regarded as effective metasis inhibitors.
The compounds of the formula I can be employed as pharmaceutical active compounds in human and veterinary medicine, in particular for the prophylaxis and/or therapy of thrombosis, myocardial infarct, arteriosclerosis, inflammations, apoplexy, angina pectoris, oncoses, osteolytic diseases such as osteoporosis, pathologically angiogenic diseases such as, for example, inflammations, ophthalmological diseases, diabetic retinopathy, macular degeneration, myopia, ocular histoplasmosis, rheumatoid arthritis, osteoarthritis, rubeotic glaucoma, ulcerative colitis, Crohn's disease, atherosclerosis, psoriasis, restenosis after angioplasty, multiple sclerosis, viral infection, bacterial infection, fungal infection, in acute kidney failure and in wound healing for supporting the healing processes.
The compounds of the formula I can be employed as substances having antimicrobial activity in operations where biomaterials, implants, catheters or heart pacemakers are used.
They have an antiseptic action here. The efficacy of the antimicrobial activity can be demonstrated by the procedure described by P. Valentin-Weigund et al., in Infection and Immunity, 2851-2855 (1988).
Since the compounds of the formula I are inhibitors of fibrinogen binding and thus ligands of the fibrinogen receptors on blood platelets, they can be used in vivo as diagnostics for the detection and localization of thrombi in the vascular system, provided they are substituted, for example, by a radioactive or UV-detectable residue.
The compounds of the formula I can be used as inhibitors of fibrinogen binding and as effective auxiliaries for the study of the metabolism of blood platelets in different activation stages or of intra-cellular signal mechanisms of the fibrinogen receptor. The detectable unit of a “label” to be incorporated, e.g. isotopic labelling by
3
H, allows, after binding to the receptor, the mechanisms mentioned to be investigated.
In the compounds of the formula I, the amino acids present can be modified such that the C
&agr;
carbon is replaced by nitrogen, with retention of the side chain. In this case, these are so-called aza-amino acids. For example, in the aza-tripeptide below, consisting of the amino acids arginine, glycine and aspartic acid, the C
&agr;
carbon of the glycine is replaced by nitrogen.
In the compounds of the formula I according to the invention, at least one amino acid is always present as an aza-amino acid.
The abbreviations of amino acid residues listed above and below stand for the radicals of the following amino acids:
Ala
alanine
Asn
asparagine
Asp
aspartic acid
Arg
arginine
Cys
cysteine
Gln
glutamine
Glu
glutamic acid
Gly
glycine
His
histidine
homo-Phe
homo-phenylalanine
Ile
isoleucine
Leu
leucine
Lys
lysine
Met
methionine
Nle
norleucine
Orn
ornithine
Phe
phenylalanine
Phg
phenylglycine
4-Hal-Phe
4-halophenylalanine
Pro
proline
Sar
sarcosine (N-methylglycine)
Ser
serine
Tic
tetrahydroisoquinoline-3-carboxylic acid
Thr
threonine
Trp
tryptophan
Tyr
tyrosine
Val
valine.
Ac
acetyl
Boc
tert-butoxycarbonyl
CBZ or Z
benzyloxycarbonyl
DCCI
dicyclohexylcarbodiimide
DIPEA
diisopropylethylamine
DMF
dimethylformamide
EDCI
N-ethyl-N,N′-(dimethylaminopropyl) carbo-
diimide
Et
ethyl
Fmoc
9-fluorenylmethoxycarbonyl
HOBt
1-hydroxybenzotriazole
Me
methyl
MBHA
4-methylbenzhydrylamine
Mtr
4-methoxy-2,3,6-trimethylphenylsulfonyl
NMP
N-methylpyrrolidone
HONSu
N-hydroxysuccinimide
OBzl
benzyl ester
OtBu
tert-butyl ester
Oct
octanoyl
OMe
methyl ester
OEt
ethyl ester
Pbf
2,2,4,6,7-pentamethyldihydrobenzofuran-
5-sulfonyl
POA
phenoxyacetyl
Sal
salicyloyl
TBTU
O-(1H-benzotriazol-1-yl)-N,N,N′,N′-tetra-
methyluronium tetrafluoroborate
TFA
trifluoroacetic acid
Trt
trityl (triphenylmethyl).
If the abovementioned amino acids can occur in several enantiomeric forms, then above and below, e.g. as a constituent of the compounds of the formula I, all these forms and also their mixtures (e.g. the DL forms) are included. Furthermore, the amino acids can be provided, e.g. as a constituent of compounds of the formula I, with corresponding protective groups which are known per se.
So-call

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