专肽生物_定制多肽合成服务_多肽合成定制服务_多肽合成厂家_多肽合成公司

This substance P analog is a very potent broad-spectrum neuropeptide inhibitor for small cell lung cancer (SCLC) cell growth in vitro (IC₅₀ = 5 µM). Moreover it potently inhibited signal transduction pathways in vitro and significantly delayed the growth of an SCLC xenograft in vivo. It could therefore be of therapeutic value in SCLC.

很多蛋白在细胞中非常容易被降解，或被标记，进而被选择性地破坏。但含有部分D型氨基酸的多肽则显示了很强的抵抗蛋白酶降解能力。

定义
酶是用于生化反应的非常有效的催化剂。它们通过提供较低活化能的替代反应途径来加快反应速度。酶作用于底物并产生产物。一些物质降低或什至停止酶的催化活性被称为抑制剂。
发现
1965年，Umezawa H分析了微生物产生的酶抑制剂，并分离出了抑制亮肽素和抗痛药的胰蛋白酶和木瓜蛋白酶，乳糜蛋白酶抑制的胰凝乳蛋白酶，胃蛋白酶抑制素抑制胃蛋白酶，泛磷酰胺抑制唾液酸酶，乌藤酮抑制酪氨酸羟化酶，多巴汀抑制多巴胺3-羟硫基嘧啶和多巴胺3-羟色胺酶酪氨酸羟化酶和多巴胺J3-羟化酶。最近，一种替代方法已应用于预测新的抑制剂：合理的药物设计使用酶活性位点的三维结构来预测哪些分子可能是抑制剂1。已经开发了用于识别酶抑制剂的基于计算机的方法，例如分子力学和分子对接。
结构特征
已经确定了许多抑制剂的晶体结构。已经确定了三种与凝血酶复合的高效且选择性的低分子量刚性肽醛醛抑制剂的晶体结构。这三种抑制剂全部在P3位置具有一个新的内酰胺部分，而对胰蛋白酶选择性最高的两种抑制剂在P1位置具有一个与S1特异性位点结合的胍基哌啶基。凝血酶的抑制动力学从慢到快变化，而对于胰蛋白酶，抑制的动力学在所有情况下都快。根据两步机理2中稳定过渡态络合物的缓慢形成来检验动力学。
埃米尔•菲舍尔（Emil Fischer）在1894年提出，酶和底物都具有特定的互补几何形状，彼此恰好契合。这称为“锁和钥匙”模型3。丹尼尔·科什兰（Daniel Koshland）提出了诱导拟合模型，其中底物和酶是相当灵活的结构，当底物与酶4相互作用时，活性位点通过与底物的相互作用不断重塑。
在众多生物活性肽的成熟过程中，需要由其谷氨酰胺（或谷氨酰胺）前体形成N末端焦谷氨酸（pGlu）。游离形式并与底物和三种咪唑衍生抑制剂结合的人QC的结构揭示了类似于两个锌外肽酶的α/β支架，但有多个插入和缺失，特别是在活性位点区域。几种活性位点突变酶的结构分析为针对QC相关疾病5的抑制剂的合理设计提供了结构基础。
作用方式
酶是催化化学反应的蛋白质。酶与底物相互作用并将其转化为产物。抑制剂的结合可以阻止底物进入酶的活性位点和/或阻止酶催化其反应。抑制剂的种类繁多，包括：非特异性，不可逆，可逆-竞争性和非竞争性。可逆抑制剂 以非共价相互作用（例如疏水相互作用，氢键和离子键）与酶结合。非特异性抑制方法包括最终使酶的蛋白质部分变性并因此不可逆的任何物理或化学变化。特定抑制剂 对单一酶发挥作用。大多数毒药通过特异性抑制酶发挥作用。竞争性抑制剂是任何与底物的化学结构和分子几何结构非常相似的化合物。抑制剂可以在活性位点与酶相互作用，但是没有反应发生。非竞争性抑制剂是与酶相互作用但通常不在活性位点相互作用的物质。非竞争性抑制剂的净作用是改变酶的形状，从而改变活性位点，从而使底物不再能与酶相互作用而产生反应。非竞争性抑制剂通常是可逆的。不可逆抑制剂与酶形成牢固的共价键。这些抑制剂可以在活性位点附近或附近起作用。
功能
工业应用中， 酶在商业上被广泛使用，例如在洗涤剂，食品和酿造工业中。蛋白酶用于“生物”洗衣粉中，以加速蛋白质在诸如血液和鸡蛋等污渍中的分解。商业上使用酶的问题包括：它们是水溶性的，这使得它们难以回收，并且一些产物可以抑制酶的活性（反馈抑制）。
药物分子，许多药物分子都是酶抑制剂，药用酶抑制剂通常以其特异性和效力为特征。高度的特异性和效力表明该药物具有较少的副作用和较低的毒性。酶抑制剂在自然界中发现，并且也作为药理学和生物化学的一部分进行设计和生产6。
天然毒物 通常是酶抑制剂，已进化为保护植物或动物免受天敌的侵害。这些天然毒素包括一些已知最剧毒的化合物。
神经气体（ 例如二异丙基氟磷酸酯（DFP））通过与丝氨酸的羟基反应生成酯，从而抑制了乙酰胆碱酯酶的活性位点。
参考
1、Scapin G (2006). Structural biology and drug discovery. Curr. Pharm. Des.,      12(17):2087–2097.
2、Krishnan R, Zhang E, Hakansson K, Arni RK, Tulinsky A, Lim-Wilby MS, Levy OE, Semple JE, Brunck TK (1998). Highly selective mechanism-based thrombin inhibitors:  structures of thrombin and trypsin inhibited with rigid peptidyl aldehydes. Biochemistry, 37 (35):12094-12103.
3、Fischer E (1894). Einfluss der configuration auf die wirkung der enzyme. Ber. Dt. Chem. Ges., 27:2985–2993.
4、Koshland DE (1958). Application of a theory of enzyme specificity to protein synthesis. PNAS., 44 (2):98–104.
5、Huang KF, Liu YL, Cheng WJ, Ko TP, Wang AH (2005). Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. PNAS., 102(37):13117-13122.
6、Holmes CF, Maynes JT, Perreault KR, Dawson JF, James MN (2002). Molecular enzymology underlying regulation of protein phosphatase-1 by natural toxins. Curr Med Chem., 9(22):1981-1989.

Definition
Enzymes are very efficient catalysts for biochemical reactions. They speed up reactions by providing an alternative reaction pathway of lower activation energy. Enzyme acts on substrate and gives rise to a product. Some substances reduce or even stop the catalytic activities of enzymes are called inhibitors.

Discovery
In 1965, Umezawa H analysed enzyme inhibitors produced by microorganisms and isolated leupeptin and antipain inhibiting trypsin and papain, chymostatin inhibiting chymotrypsin, pepstatin inhibiting pepsin, panosialin inhibiting sialidases, oudenone inhibiting tyrosine hydroxylase, dopastin inhibiting dopamine 3-hydroxylase, aquayamycin and chrothiomycin inhibiting tyrosine hydroxylase and dopamine J3-hydroxylase . Recently, an alternative approach has been applied to predict new inhibitors: rational drug design uses the three-dimensional structure of an enzyme's active site to predict which molecules might be inhibitors 1. Computer-based methods for identifying inhibitor for an enzyme have been developed, such as molecular mechanics and molecular docking.

Structural Characteristics
The crystal structures of many inhibitors have been determined. The crystal structures of three highly potent and selective low-molecular weight rigid peptidyl aldehyde inhibitors complexed with thrombin have been determined. All the three inhibitors have a novel lactam moiety at the P3 position, while the two with greatest trypsin selectivity have a guanidinopiperidyl group at the P1 position that binds in the S1 specificity site. The kinetics of inhibition vary from slow to fast with thrombin and are fast in all cases with trypsin. The kinetics are examined in terms of the slow formation of a stable transition-state complex in a two-step mechanism 2.

Emil Fischer in 1894 suggested that both the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another.This is known as "the lock and key" model 3. Daniel Koshland suggested induced fit model where substrate and enzymes are rather flexible structures, the active site is continually reshaped by interactions with the substrate as the substrate interacts with the enzyme 4.

N-terminal pyroglutamate (pGlu) formation from its glutaminyl (or glutamyl) precursor is required in the maturation of numerous bioactive peptides. The structure of human QC in free form and bound to a substrate and three imidazole-derived inhibitors reveals an alpha/beta scaffold akin to that of two-zinc exopeptidases but with several insertions and deletions, particularly in the active-site region. The structural analyses of several active-site-mutant enzymes provide a structural basis for the rational design of inhibitors against QC-associated disorders 5.

Mode of Action
Enzymes are proteins that catalyze chemical reactions. Enzymes interact with substrate and convert them into products. Inhibitor binding can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalyzing its reaction. There are a variety of types of inhibitors including: nonspecific, irreversible, reversible - competitive and noncompetitive. Reversible inhibitors bind to enzymes with non-covalent interactions like hydrophobic interactions, hydrogen bonds, and ionic bonds. Non-specific methods of inhibition include any physical or chemical changes which ultimately denature the protein portion of the enzyme and are therefore irreversible. Specific Inhibitors exert their effects upon a single enzyme. Most poisons work by specific inhibition of enzymes. A competitive inhibitor is any compound which closely resembles the chemical structure and molecular geometry of the substrate. The inhibitor may interact with the enzyme at the active site, but no reaction takes place. A noncompetitive inhibitor is a substance that interacts with the enzyme, but usually not at the active site.  The net effect of a non competitive inhibitor is to change the shape of the enzyme and thus the active site, so that the substrate can no longer interact with the enzyme to give a reaction. Non competitive inhibitors are usually reversible. Irreversible Inhibitors form strong covalent bonds with an enzyme.  These inhibitors may act at, near, or remote from the active site .

Functions
Industrial application, enzymes are widely used commercially, for example in the detergent, food and brewing industries. Protease enzymes are used in 'biological' washing powders to speed up the breakdown of proteins in stains like blood and egg. Problems using enzymes commercially include: they are water soluble which makes them hard to recover and some products can inhibit the enzyme activity (feedback inhibition) .

Drug molecules, many drug molecules are enzyme inhibitors and a medicinal enzyme inhibitor is usually characterized by its specificity and its potency. A high specificity and potency suggests that a drug will have fewer side effects and less toxic. Enzyme inhibitors are found in nature and are also designed and produced as part of pharmacology and biochemistry 6.

Natural poisons are often enzyme inhibitors that have evolved to defend a plant or animal against predators. These natural toxins include some of the most poisonous compounds known.

Nerve gases such as diisopropylfluorophosphate (DFP) inhibit the active site of acetylcholine esterase by reacting with the hydroxyl group of serine to make an ester.

References

Scapin G (2006). Structural biology and drug discovery. Curr. Pharm. Des.,      12(17):2087–2097.

Krishnan R, Zhang E, Hakansson K, Arni RK, Tulinsky A, Lim-Wilby MS, Levy OE, Semple JE, Brunck TK (1998). Highly selective mechanism-based thrombin inhibitors:  structures of thrombin and trypsin inhibited with rigid peptidyl aldehydes. Biochemistry, 37 (35):12094-12103.

Fischer E (1894). Einfluss der configuration auf die wirkung der enzyme. Ber. Dt. Chem. Ges., 27:2985–2993.

Koshland DE (1958). Application of a theory of enzyme specificity to protein synthesis. PNAS., 44 (2):98–104.

Huang KF, Liu YL, Cheng WJ, Ko TP, Wang AH (2005). Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. PNAS., 102(37):13117-13122.

Holmes CF, Maynes JT, Perreault KR, Dawson JF, James MN (2002). Molecular enzymology underlying regulation of protein phosphatase-1 by natural toxins. Curr Med Chem., 9(22):1981-1989.

定义
物质P（SP）是十一肽，在周围和中枢神经系统中都丰富，通常与一种经典的神经递质之一，最常见的是血清素（5-HT）^1共定位。

相关肽
SP属于神经肽家族，称为速激肽，具有共同的C端序列：Phe-X-Gly-Leu-Met-NH ₂。三种最常见的速激肽是SP，神经激肽A（NKA）和神经激肽B（NKB）。它们的生物学作用是通过称为NK1，NK2和NK3的特定细胞表面受体介导的，其中SP是NK1受体的首选激动剂，NKA是NK2受体的首选激动剂，NKB是NK3受体的²激动剂。

Discovery
SP最初是由冯·欧拉（von Euler）和加德姆（Gaddum）于1931年发现的，是一种引起体外肠道收缩的组织提取物。在随后的几十年中，它的生物活性和组织分布得到了进一步的研究³。

结构特征
SP是具有11个残基的神经肽，序列为Arg-Pro-Lys-Pro-Gln-Glin-Phe-Gly-Leu-Met-NH ₂）⁴。在一项研究中，将SP的C和N末端片段与母体分子在以下方面的能力进行了比较：（a）收缩分离的豚鼠回肠，（b）在大鼠中诱导唾液分泌，（c）激发单只猫背角神经元，以及（d）通过小鼠颅内注射诱导抓挠。在所有测定系统中，与七肽一样小的C末端片段都是有效的SP激动剂。包含五个或更少氨基酸的C末端片段至多仅具有弱活性。N-末端片段在分离的豚鼠回肠上完全没有活性。然而，在大鼠唾液分泌和中枢神经系统分析中，N末端片段具有弱的SP样活性⁵。获得的结果表明，尽管SP的羧基末端对于肽支气管活性是必不可少的，但是氨基末端肽的丢失（最多四个残基）实际上增强了对肽的支气管收缩剂反应。这种增强的一部分似乎是由SP和SP5-11的酶促降解差异引起的。数据表明，二肽基氨基肽酶对SP的切割可以增强其生物活性⁶。SP类似物：Senktide（琥珀酰-[Asp6，Me-Phe8] SP-（6-11））是NK-3（SP-N）受体的选择性类似物，效力比SP高20-100倍，约为1000倍比为NK-1（SP-P）受体选择性类似物，其驻留在肌肉细胞更有效的⁷。鞘内注射后研究了5种SP类似物对神经激肽（NK）1受体激动剂如SP，藻蛋白和（p-Glu6，Pro9）-SP（6-11）（肽）诱导的舔，咬和scratch痒反应的影响。在小鼠中。肽引起类似SP的行为反应，其效力是D-Pro9类似物D-肽的25倍。（D-Arg1，D-Pro2,4，D-Phe7，D-His9，Leu11）-SP的剂量低于（D-Phe7，D-His9，Leu11）-SP的肽诱导的应答（6 -11）。相反，（D-Arg1，D-Pro2,4，D-Phe7，D-His9）-SP（0.5-1.0 nmol）和（D-Phe7，D-His9）-SP（6-11）（0.5- 2.0 nmol）仅抑制SP诱导的行为反应，而不抑制physalaemin或肽诱导的反应。⁸。P物质[D-Arg1，D-Phe5，D-Trp7,9，Leu11] SP（SpD）和[Arg6，D-Trp7,9，NmePhe8]类似物P可以抑制神经肽刺激的Ca2 +动员，酪氨酸磷酸化和ERK激活。至关重要的是，SpD和[Arg6，D-Trp7,9，NmePhe8] SP在体内和体外均抑制SCLC细胞生长并刺激SCLC细胞凋亡。SP类似物最初被表征为“广谱神经肽拮抗剂” ⁹。

作用方式
SP受体是一种G蛋白偶联受体，在许多方面与精神病学中其他经过充分研究的受体相似，特别是单胺受体²。SP与其受体的相互作用激活了Gq，Gq又激活了磷脂酶C，将磷脂酰肌醇双磷酸酯分解为肌醇三磷酸酯（IP3）和二酰基甘油（DAG）。IP3作用于肌质网中的特定受体以释放Ca2 +的细胞内储存，而DAG通过蛋白激酶C作用以打开质膜中的L型钙通道。细胞内[Ca2 +]的升高诱导组织反应。与SP所见的一系列动作一样，存在多种治疗可能性¹⁰。

功能
在中枢神经系统中，SP与情绪障碍，焦虑，压力，增强，神经发生，神经毒性和疼痛的调节有关。在消化道，SP，以及一些其他速激肽，是神经递质，调节运动活动，离子和液体的分泌，以及血管功能^11，12。

参考

1. Argyropoulos SV, Nutt DJ (2000). Substance P antagonists: novel agents in the treatment of depression. Expert Opin Investig Drugs,  9(8):1871-1875.
2. Book: Substance P and Related Tachykinins. Chapter 13: Neuropsychopharmacology: By Nadia MJ, Kramer MS.
3. Senba E, Tohyama M (1985). Origin and fine structure of substance P-containing nerve terminals in the facial nucleus of the rat:an immunohistochemical study. Exp Brain Res., 57(3):537-546.
4. Seidel MF, Tsalik J, Vetter H, Müller W (2007). Substance P in Rheumatic Diseases. Current Rheumatology Reviews, 3:17-30.
5. Piercey MF, Dobry PJ, Einspahr FJ, Schroeder LA, Masiques N (1982) Use of substance P fragments to differentiate substance P receptors of different tissues. Regulatory Peptides, 3(5-6):337-349.
6. Shore SA, Drazen JM (1988). Airway responses to substance P and substance P fragments in the guinea pig. Pulm Pharmacol., 1(3):113-118.
7. Hanani M, Chorev M, Gilon C, Selinger Z (1988). The actions of receptor-selective substance P analogs on myenteric neurons: an electrophysiological investigation. European journal of pharmacology, 153(2-3):247-253.
8. Sakurada T, Yamada T, Tan-no K, Manome Y, Sakurada S, Kisara K, Ohba M (1991). Differential effects of substance P analogs on neurokinin 1 receptor agonists in the mouse spinal cord. J Pharmacol Exp Ther.,  259:205-210
9. MacKinnon AC, Waters C, Jodrell D, Haslett C, Sethi T (2001). Bombesin and Substance P Analogues Differentially Regulate G-protein Coupling to the Bombesin Receptor. J. Biol. Chem.,   276(30):28083-28091..
10. Khawaja AM, Rogers DF (1996). Tachykinins: receptor to effector. Int J Biochem Cell Biol.,  28(7):721-738.
11.  Leeman SE, Mroz EA (1974).  Substance P. Life Sci., 15(12):2033–2044.
12. Wiesenfeld-Hallin Z, Xu XJ (1993). The differential roles of substance P and neurokinin A in spinal cord hyperexcitability and neurogenic inflammation. Regul Pept., 46(1-2):165-173

多肽H2N-DArg-Pro-Lys-Pro-DTrp-Gln-DTrp-Phe-DTrp-Leu-Leu-NH2的合成步骤：

1、合成MBHA树脂：取若干克的MBHA树脂（如初始取代度为0.5mmol/g）和1倍树脂摩尔量的Fmoc-Linker-OH加入到反应器中，加入DMF，搅拌使氨基酸完全溶解。再加入树脂2倍量的DIEPA，搅拌混合均匀。再加入树脂0.95倍量的HBTU，搅拌混合均匀。反应3-4小时后，用DMF洗涤3次。用2倍树脂体积的10%乙酸酐/DMF 进行封端30分钟。然后再用DMF洗涤3次，甲醇洗涤2次，DCM洗涤2次，再用甲醇洗涤2次。真空干燥12小时以上，得到干燥的树脂{Fmoc-Linker-MHBA Resin}，测定取代度。这里测得取代度为 0.3mmol/g。结构如下图：

2、脱Fmoc：取1.35g的上述树脂，用DCM或DMF溶胀20分钟。用DMF洗涤2遍。加3倍树脂体积的20%Pip/DMF溶液，鼓氮气30分钟，然后2倍树脂体积的DMF 洗涤5次。得到 H2N-Linker-MBHA Resin 。（此步骤脱除Fmoc基团，茚三酮检测为蓝色，Pip为哌啶）。结构图如下：

3、缩合：取1.22mmol Fmoc-Leu-OH 氨基酸，加入到上述树脂里，加适当DMF溶解氨基酸，再依次加入2.43mmol DIPEA，1.15mmol HBTU。反应30分钟后，取小样洗涤，茚三酮检测为无色。用2倍树脂体积的DMF 洗涤3次树脂。（洗涤树脂，去掉残留溶剂，为下一步反应做准备）。得到Fmoc-Leu-Linker-MBHA Resin。氨基酸：DIPEA：HBTU：树脂=3：6：2.85：1（摩尔比）。结构图如下：

4、依次循环步骤二、步骤三，依次得到

H2N-Leu-Linker-MBHA Resin

Fmoc-Leu-Leu-Linker-MBHA Resin

H2N-Leu-Leu-Linker-MBHA Resin

Fmoc-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-Lys(Boc)-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-Lys(Boc)-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-Pro-Lys(Boc)-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

H2N-Pro-Lys(Boc)-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

Fmoc-DArg(Pbf)-Pro-Lys(Boc)-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin

以上中间结构，均可在专肽生物多肽计算器-多肽结构计算器中，一键画出。

最后再经过步骤二得到 H2N-DArg(Pbf)-Pro-Lys(Boc)-Pro-DTrp(Boc)-Gln(Trt)-DTrp(Boc)-Phe-DTrp(Boc)-Leu-Leu-Linker-MBHA Resin，结构如下：

5、切割：6倍树脂体积的切割液（或每1g树脂加8ml左右的切割液），摇床摇晃 2小时，过滤掉树脂，用冰无水乙醚沉淀滤液，并用冰无水乙醚洗涤沉淀物3次，最后将沉淀物放真空干燥釜中，常温干燥24小试，得到粗品H2N-DArg-Pro-Lys-Pro-DTrp-Gln-DTrp-Phe-DTrp-Leu-Leu-NH2。结构图见产品结构图。

切割液选择：1）TFA：H2O=95%：5%

2）TFA：H2O：TIS=95%：2.5%：2.5%

3）三氟乙酸：茴香硫醚：1，2-乙二硫醇：苯酚：水=87.5%：5%：2.5%：2.5%：2.5%

（前两种适合没有容易氧化的氨基酸，例如Trp、Cys、Met。第三种适合几乎所有的序列。）

6、纯化冻干：使用液相色谱纯化，收集目标峰液体，进行冻干，获得蓬松的粉末状固体多肽。不过这时要取小样复测下纯度 是否目标纯度。

7、最后总结：

杭州专肽生物技术有限公司（ALLPEPTIDE https://www.allpeptide.com）主营定制多肽合成业务，提供各类长肽，短肽，环肽，提供各类修饰肽，如：荧光标记修饰（CY3、CY5、CY5.5、CY7、FAM、FITC、Rhodamine B、TAMRA等），功能基团修饰肽（叠氮、炔基、DBCO、DOTA、NOTA等），同位素标记肽（N15、C13），订书肽（Stapled Peptide）,脂肪酸修饰肽（Pal、Myr、Ste），磷酸化修饰肽（P-Ser、P-Thr、P-Tyr），环肽（酰胺键环肽、一对或者多对二硫键环），生物素标记肽，PEG修饰肽，甲基化修饰肽等。

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