PSSJ（日本蛋白質科学会） – 第18回年会に参加しました

著者 Malvern Panalytical, Wednesday, 1st August 2018

Malvern Panaritical participated in “The 18th Annual Meeting of the Japanese Society for Protein Science (PSSJ)” held at Niigata · Toki Messe from June 26 to 28, 2018. In this blog, a summary of the luncheon seminar “Data comparison of model proteins by size analysis method in several solutions” and “Capture interaction mode of natural denatured protein using thermo-measurement ITC” and the state of the exhibition booth I will report it.

We would like to take this opportunity to express our gratitude to everyone who came to the two luncheon seminars and the exhibition booth.

Luncheon Seminar 1: Comparison of model protein data by size analysis method in several solutions

At the luncheon seminar on 26th June, entitled “Data Comparison of Model Protein by Size Analysis Method in Some Solution”, GPC-LS, dynamic light scattering method (DLS) , Taylor dispersion method (TDA) , X ray Secondary virial coefficient (B22) obtained from it, the diffusion coefficient (B22) obtained from the size of the protein (particle diameter) obtained using various measurement principles such as small angle scattering method (SAXS) We introduced parameters such as concentration dependence (kD) and its comparison. In addition, we discussed the relationship between these parameters and the viscosity and the occurrence of SVP (sub-bibulous particles, protein aggregates) for the state of high concentration required for antibody drugs.

The state of the luncheon seminar (June 28)

Luncheon Seminar 1: Overview

June 26 (Tue) 12: 00 ~ 12: 50 E venue (medium conference room 201) 1
LSE Comparison of model protein data by several solution size analysis
Data comparison with various principles for protein size in solution
Malvern Panari Tikal (Spectris Co.) Shiwa Kohei

Kohei Shiba, Malvern Panalytical, A division of Spectris Co., Ltd.　

Luncheon Seminar 1: Summary　

“It is widely known that each protein has a unique structure and exhibits its function by maintaining its structure, so information on proteins in solution becomes important information when considering the relationship with function Among them, size information is expected to directly link changes in higher order structure, and most of the physical property analysis in solution contains information on interactions occurring between proteins. , And in industrial, specifically protein and pharmaceuticals, these cases are increasingly being used to predict the dispersion stability of these parameters.

There are several methods for analyzing the size in solution, and the information derived from each principle has its own characteristics.

Dynamic light scattering method (DLS) observes changes in scattering intensity when laser light is irradiated on a sample solution, so you can see the entire nano size range, but also for other details in order to obtain more detailed information Is desirable.
Even with the same light scattering method, the light scattering detector (GPC – LS) connected with liquid chromatography can be combined with information such as conformational change by combining the separation capability of liquid chromatography and absolute value measurement by light scattering method I can.
Taylor分散法（TDA）は、キャピラリ泳動法を用いて拡散係数/流体力学的サイズを求める原理です。この原理はDLSに比べ、シングルナノサイズの精度に優れ、サイズ変化Kinetics解析に向いている手法と考えられます。
また、X線小角散乱法（SAXS）は、分子量や溶液中の形状を算出することができます。本発表では、上で挙げたDLS、GPC-LS、TDAおよびSAXSについて、それぞれからどのような情報が得られるのかについて、アプリケーション事例を通じて紹介します。また、産業的応用として、蛋白質医薬品の安定性予測の具体的事例についても触れます。」

各装置の原理と特徴

ランチョンセミナー 2：いくつかの溶液中サイズ解析法によるモデル蛋白質のデータ比較

2日目のランチョンセミナーでは、東京大学医科学研究所の長門石暁先生にご講演いただきました。先生からは、天然変性タンパク質をモデルとして、その結合対象との認識機構の解明をHDX-MSと当社製品 MicroCal ITCを組み合わせて行った事例をご紹介いただきました。

ランチョンセミナー2：概要

6 月 27 日（水）　12:00 ～ 12:50　E 会場（中会議室 201）
2LSE　熱測定 ITC を活用して天然変性蛋白質の相互作用様式を捉える
Elucidation of binding manner for an intrinsically disordered protein using ITC
東京大学　長門石暁
Satoru Nagatoishi, The University of Tokyo

ランチョンセミナー2：講演要旨　

「天然変性蛋白質は単独の溶液中では特定の高次構造を持たないが、相方となる蛋白質と特異的に相互作用し、場合によっては結合によって二次構造を形成する例も報告されています。しかし初期状態において明確な構造を形成していないために、その相互作用メカニズムやそれに伴う分子レベルでの機能を予測することは困難です。

したがって天然変性蛋白質の分子認識機構に関する詳細、特に物理化学的知見は未だ未解明な点が多くあります。複合体構造を議論する上で威力を発揮しているX線結晶構造解析は有力なツールの１つでありますが、天然変性蛋白質の高いフレキシビリティーにより共結晶を得ることは容易ではなく、結果として断片化しペプチドレベルにまで低分子化することを余儀なくされ、蛋白質の全体像を捉えるには至っていません。やはり溶液中で蛋白質―蛋白質間相互作用、その複合体に関する分子レベルでの詳細な情報を得る必要があり、結晶解析と溶液解析のコンビネーションによって、より正確な構造情報と相互作用様式を議論することが重要であります。

本研究では、嫌気的環境下において代謝異常を引き起こし、がん細胞の生存・増殖を助けることが知られている天然変性蛋白質Mint3をモデルとして、その結合対象であるホモダイマー型FIH-1に対する認識機構の解明を、等温滴定型熱量測定（ITC）を用いて試みました。

Mint3はFIH-1に対して1：2の結合量論比を有する発熱反応の相互作用が観察されました。またMint3を断片化することにより、結合自由エネルギーに貢献するコア領域の絞り込みにも成功しました。さらに重水素交換質量分析法HDX-MSを組み合わせることにより、Mint3はFIH-1全体を覆うような結合様式をとることが示唆され、Mint3のFIH-1に対する機能抑制メカニズムをより明確にすることができました。

In this way, we succeeded in grasping the mode of interaction in solution of natural denatured protein using ITC . ITC is considered to be a powerful analytical tool that provides useful knowledge and guidance in the search and design of inhibitors targeted to native denatured protein, which is still considered to be difficult . “

Exhibition booth

The exhibition booth was a place that was very easy to understand as soon as I entered the poster exhibition hall entrance, so many visitors came.

In the booth, we introduced examples of physical property analysis of antibody drugs, protein size measurement, and thermal measurement. In addition, the Zetasizer Pro / Ultra , a new product particle size / zeta potential measurement device of dynamic light scattering method / electrophoretic light scattering method　also exhibited actual equipment and received many inquiries from many customers.

Estimate Request　/　Demo Request　/　Sales Contact

Past Exhibit Information

For past exhibition information, please click here.

The 17th Annual Meeting of the Japanese Protein Science Association, 2017

Malvern will participate in the 17th Annual Meeting of The Japanese Society for Protein Science.
This year, we will expand Malvern ‘s booth from last year. In addition, the luncheon seminar was held for two days. We will talk to professors who are professionals of protein analysis.

Tickets for each luncheon seminar will be handed over to each first-come, first served basis.

The 17th Annual Meeting of the Protein Science Association of Japan

Date and time June 20 (Tue) – 22 (Thursday), 2017
Venue: Sendai International Center

Luncheon Seminar

June 20 (Tuesday) 1 LSE Malvern (Spectris Co., Ltd.)
　Thermodynamics of interaction between proteins using isothermal titration thermal measurement　
　Osaka University protein research laboratory Lee Hyo-hae
　Venue: E venue (Exhibition building meeting room 4) 12: 00-12: 50
June 21 (Wed) 2 LSE Malvern (Spectris, Inc.)
　Stabilization strategy based on understanding of protein solution physical properties
　Osaka University Graduate School of Engineering / Okazaki Integrated Bio / Professor Uchiyama Susumu of Guangdong Institute of Technology
　Venue: E Venue (Exhibition Hall Conference Room 4) 12: 00-12: 50

Exhibited products

A new product MicroCal PEAQ – DSC will also be exhibited. Also, Malvern’s full-time academic staff will introduce the product, so please drop in.

Thermal stability analyzer Differential scanning microcalorimeter MicroCal PEAQ-DSC
Intermolecular interaction analyzer isothermal titration calorimeter MicroCal PEAQ-ITC

Panel display

Particle diameter · Zeta potential · Molecular weight measurement device Zetasizer Nano series

Micro viscosity / size measurement device Viscosizer TD